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Showing posts with label Medical Science. Show all posts
Showing posts with label Medical Science. Show all posts

Friday, 3 April 2020

Trial drug can significantly block early stages of COVID-19 in engineered human tissues


An international team led by University of British Columbia researcher Dr. Josef Penninger has found a trial drug that effectively blocks the cellular door SARS-CoV-2 uses to infect its hosts.

The findings, published today in Cell, hold promise as a treatment capable of stopping early infection of the novel coronavirus that, as of April 2, has affected more than 981,000 people and claimed the lives of 50,000 people worldwide.

The study provides new insights into key aspects of SARS-CoV-2, the virus that causes COVID-19, and its interactions on a cellular level, as well as how the virus can infect blood vessels and kidneys.

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"We are hopeful our results have implications for the development of a novel drug for the treatment of this unprecedented pandemic," says Penninger, professor in UBC's faculty of medicine, director of the Life Sciences Institute and the Canada 150 Research Chair in Functional Genetics at UBC.

"This work stems from an amazing collaboration among academic researchers and companies, including Dr. Ryan Conder's gastrointestinal group at STEMCELL Technologies in Vancouver, Nuria Montserrat in Spain, Drs. Haibo Zhang and Art Slutsky from Toronto and especially Ali Mirazimi's infectious biology team in Sweden, who have been working tirelessly day and night for weeks to better understand the pathology of this disease and to provide breakthrough therapeutic options."



ACE2 -- a protein on the surface of the cell membrane -- is now at centre-stage in this outbreak as the key receptor for the spike glycoprotein of SARS-CoV-2. In earlier work, Penninger and colleagues at the University of Toronto and the Institute of Molecular Biology in Vienna first identified ACE2, and found that in living organisms, ACE2 is the key receptor for SARS, the viral respiratory illness recognized as a global threat in 2003. His laboratory also went on to link the protein to both cardiovascular disease and lung failure.

While the COVID-19 outbreak continues to spread around the globe, the absence of a clinically proven antiviral therapy or a treatment specifically targeting the critical SARS-CoV-2 receptor ACE2 on a molecular level has meant an empty arsenal for health care providers struggling to treat severe cases of COVID-19.

"Our new study provides very much needed direct evidence that a drug -- called APN01 (human recombinant soluble angiotensin-converting enzyme 2 -- hrsACE2) -- soon to be tested in clinical trials by the European biotech company Apeiron Biologics, is useful as an antiviral therapy for COVID-19," says Dr. Art Slutsky, a scientist at the Keenan Research Centre for Biomedical Science of St. Michael's Hospital and professor at the University of Toronto who is a collaborator on the study.

In cell cultures analyzed in the current study, hrsACE2 inhibited the coronavirus load by a factor of 1,000-5,000. In engineered replicas of human blood vessel and kidneys -- organoids grown from human stem cells -- the researchers demonstrated that the virus can directly infect and duplicate itself in these tissues. This provides important information on the development of the disease and the fact that severe cases of COVID-19 present with multi-organ failure and evidence of cardiovascular damage. Clinical grade hrsACE2 also reduced the SARS-CoV-2 infection in these engineered human tissues.

"Using organoids allows us to test in a very agile way treatments that are already being used for other diseases, or that are close to being validated. In these moments in which time is short, human organoids save the time that we would spend to test a new drug in the human setting," says Nรบria Montserrat, ICREA professor at the Institute for Bioengineering of Catalonia in Spain.



"The virus causing COVID-19 is a close sibling to the first SARS virus," adds Penninger. "Our previous work has helped to rapidly identify ACE2 as the entry gate for SARS-CoV-2, which explains a lot about the disease. Now we know that a soluble form of ACE2 that catches the virus away, could be indeed a very rational therapy that specifically targets the gate the virus must take to infect us. There is hope for this horrible pandemic."

This research was supported in part by the Canadian federal government through emergency funding focused on accelerating the development, testing, and implementation of measures to deal with the COVID-19 outbreak.


Bibliography:

Vanessa Monteil, Hyesoo Kwon, Patricia Prado, Astrid Hagelkrรผys, Reiner A. Wimmer, Martin Stahl, Alexandra Leopoldi, Elena Garreta, Carmen Hurtado Del Pozo, Felipe Prosper, J.p. Romero, Gerald Wirnsberger, Haibo Zhang, Arthur S. Slutsky, Ryan Conder, Nuria Montserrat, Ali Mirazimi, Josef M. Penninger.

Inhibition of SARS-CoV-2 infections in engineered human tissues using clinical-grade soluble human ACE2.

Submitted to Cell, 2020

DOI: 10.1016/j.cell.2020.04.004

New Nanosensors could offer early detection of lung tumors


People who are at high risk of developing lung cancer, such as heavy smokers, are routinely screened with computed tomography (CT), which can detect tumors in the lungs. However, this test has an extremely high rate of false positives, as it also picks up benign nodules in the lungs.

Researchers at Massachusetts Institute of Technology (MIT) have developed a nanoparticle-based approach that allows the early diagnosis of lung cancer through a simple urine test. The strategy detects biomarkers resulting from the interaction of peptide-coated nanoparticles with disease-associated proteases in the tumor microenvironment.

Experiments in two different mouse models of lung cancer showed that the urine test could detect tumors as small as 2.8 mm3. The researchers hope that this type of noninvasive diagnosis could reduce the number of false positives associated with an existing test method, and help to detect more tumors in the early stages of the disease.

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“If you look at the field of cancer diagnostics and therapeutics, there’s a renewed recognition of the importance of early cancer detection and prevention,” said study lead Sangeeta Bhatia, PhD, who is the John and Dorothy Wilson professor of health sciences and technology and electrical engineering and computer science, and a member of MIT’s Koch Institute for Integrative Cancer Research and the Institute for Medical Engineering and Science. “We really need new technologies that are going to give us the capability to see cancer when we can intercept it and intervene early.” Bhatia and colleagues report on development of the test in Science Translational Medicine Journal.

MIT engineers have developed nanoparticles that can be delivered to the lungs, where tumor-associated proteases cut peptides on the surface of the particles, releasing reporter molecules. Those reporters can be detected by a urine test.

Lung cancer is the most common cause of cancer-related death (25.3%) in the United States the authors wrote, and has a “dismal” five-year survival rate of 18.6%. Early detection is key, as the five-year survival rates are 6- to 13-fold higher in patients whose tumors are detected before they spread to distal sites in the body. People in the United States who are at high risk of developing lung cancer, such as heavy smokers, are routinely screened using low-dose computed tomography (LDCT), which can detect tumors in the lungs.

However, this test has an extremely high rate of false positives, as it also picks up benign nodules in the lungs. There is then a “considerable burden of complications incurred during unnecessary follow-up procedures,” the investigators stated, and the method isn’t routinely used in other countries. “As a result of these complications, screening by LDCT has not been widely adopted outside of the United States, and there is “an urgent need to develop diagnostic tests that increase the effectiveness of lung cancer screening.”

The approach taken by the MIT researchers is based on the use of what they call “activity-based sensors” that monitor for disease and intensify disease-associated signals, which can then be detected in urine. “Activity-based nanosensors leverage dysregulated protease activity to overcome the insensitivity of previous biomarker assays, amplifying disease-associated signals generated in the tumor microenvironment and providing a concentrated urine-based readout,” the team explained.



Bhatia’s lab has for several years been developing such nanoparticles that can detect cancer by interacting with proteases. These enzymes help tumor cells to escape their original locations by cutting through proteins of the extracellular matrix. To find the cancer-associated proteases Bhatia created nanoparticles coated with peptides that are targeted by the cancer-related proteases. The particles accumulate at tumor sites, where the peptides are cleaved, releasing biomarkers that can then be detected in a urine sample.

The Bhatia lab has previously developed sensors for colon and ovarian cancer, and in their new study, the researchers applied the technology to lung cancer, which kills about 150,000 people in the United States every year. They project that the test could be applied to confirm cancer in patients who have had a positive CT scan. These patients would commonly undergo a biopsy or other invasive test to search for lung cancer, but in some cases, this procedure can cause complications, so a noninvasive follow-up test could be useful to determine which patients actually need a biopsy, Bhatia said.

“The CT scan is a good tool that can see a lot of things,” she said. “The problem with it is that 95% of what it finds is not cancer, and right now you have to biopsy too many patients who test positive.”

To customize their sensors for lung cancer, the researchers analyzed data in The Cancer Genome Atlas, and identified proteases that are abundant in lung cancer. They created a panel of 14 peptide-coated nanoparticles that could interact with these enzymes.

The researchers then tested the sensors in two different genetic mouse models, “driven by either Kras/Trp53 (KP) mutations, or Eml4-Alk (EA) fusion,” that spontaneously develop lung cancer. To help prevent background noise that could come from other organs or the bloodstream, the researchers injected the particles directly into the animals’ airways. The researchers carried out their diagnostic test using the sensors at 5 weeks, 7.5 weeks, and 10.5 weeks after tumor growth began. To make the diagnoses more accurate, they used machine learning to train an algorithm to distinguish between data from mice that had tumors and from mice that did not.

Using this approach, the researchers found that they could accurately detect tumors in one of the mouse models as early as 7.5 weeks, when the tumors were only 2.8 mm3, on average. In the other strain of mice, tumors could be detected at 5 weeks. The sensors’ success rate was also comparable to or better than the success rate of CT scans performed at the same time points.

“Intrapulmonary administration of the nanosensors to a Kras- and Trp53-mutant lung adenocarcinoma mouse model confirmed the role of metalloproteases in lung cancer and enabled accurate detection of localized disease, with 100% specificity and 81% sensitivity,” they reported. “Furthermore, this approach generalized to an alternative autochthonous model of lung adenocarcinoma, where it detected cancer with 100% specificity and 95% sensitivity and was not confounded by lipopolysaccharide-driven lung inflammation.”

Importantly, the sensors could distinguish between early-stage cancer and noncancerous inflammation of the lungs, a common condition in smokers, and one of the reasons that CT scans produce so many false positives. “Activity-based nanosensors may have clinical utility as a rapid, safe, and cost-effective follow-up to LDCT, reducing the number of patients referred for invasive testing,” the authors concluded. “With further optimization and validation studies, activity-based nanosensors may one day provide an accurate, noninvasive, and radiation-free strategy for lung cancer testing.”

The authors acknowledged that their study was carried out in mouse models, which do not fully recapitulate human disease, and there were other study limitations that will need to be addressed. Clinical trials will be needed to fully validate the use of activity-based nanosensors for detecting lung cancer and distinguishing malignant from benign and extrapulmonary disease, they pointed out.



Bhatia envisions that the nanoparticle sensors could be used as a noninvasive diagnostic for people who get a positive result on a screening test, potentially eliminating the need for a biopsy. For use in humans, her team is working on a form of the particles that could be inhaled as a dry powder or through a nebulizer. Another possible application is using the sensors to monitor how well lung tumors respond to treatment, such as drugs or immunotherapies. “A great next step would be to take this into patients who have known cancer, and are being treated, to see if they’re on the right medicine,” Bhatia said.


Bibliography:

Urinary detection of lung cancer in mice via noninvasive pulmonary protease profiling

Jesse D. Kirkpatrick, Andrew D. Warren, Ava P. Soleimany, Peter M. K. Westcott1, Justin C. Voog, Carmen Martin-Alonso, Heather E. Fleming, Tuomas Tammela, Tyler Jacks and Sangeeta N. Bhatia.

Science Translational Medicine  01 Apr 2020:
Vol. 12, Issue 537, eaaw0262

DOI: 10.1126/scitranslmed.aaw0262

Friday, 27 March 2020

New mathematical model can more effectively track epidemics



As COVID-19 spreads worldwide, leaders are relying on mathematical models to make public health and economic decisions.

A new model developed by Princeton and Carnegie Mellon researchers improves tracking of epidemics by accounting for mutations in diseases. Now, the researchers are working to apply their model to allow leaders to evaluate the effects of countermeasures to epidemics before they deploy them.

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“We want to be able to consider interventions like quarantines, isolating people, etc., and then see how they affect an epidemic’s spread when the pathogen is mutating as it spreads,” said H. Vincent Poor, one of the researchers on this study and Princeton’s interim dean of engineering.

The models currently used to track epidemics use data from doctors and health workers to make predictions about a disease’s progression. Poor, the Michael Henry Strater University Professor of Electrical Engineering, said the model most widely used today is not designed to account for changes in the disease being tracked. This inability to account for changes in the disease can make it more difficult for leaders to counter a disease’s spread. Knowing how a mutation could affect transmission or virulence could help leaders decide when to institute isolation orders or dispatch additional resources to an area.



“In reality, these are physical things, but in this model, they are abstracted into parameters that can help us more easily understand the effects of policies and of mutations,” Poor said.

If the researchers can correctly account for measures to counter the spread of disease, they could give leaders critical insights into the best steps they could take in the face of pandemics. The researchers are building on work published March 17 in the Proceedings of the National Academy of Sciences. In that article, they describe how their model is able to track changes in epidemic spread caused by mutation of a disease organism. The researchers are now working to adapt the model to account for public health measures taken to stem an epidemic as well.

The researchers’ work stems from their examination of the movement of information through social networks, which has remarkable similarities to the spread of biological infections. Notably, the spread of information is affected by slight changes in the information itself. If something becomes slightly more exciting to recipients, for example, they might be more likely to pass it along or to pass it along to a wider group of people. By modeling such variations, one can see how changes in the message change its target audience.

“The spread of a rumor or of information through a network is very similar to the spread of a virus through a population,” Poor said. “Different pieces of information have different transmission rates. Our model allows us to consider changes to information as it spreads through the network and how those changes affect the spread.”

“Our model is agnostic with regard to the physical network of connectivity among individuals,” said Poor, an expert in the field of information theory whose work has helped establish modern cellphone networks. “The information is being abstracted into graphs of connected nodes; the nodes might be information sources or they might be potential sources of infection.”



Obtaining accurate information is extremely difficult during an ongoing pandemic when circumstances shift daily, as we have seen with the COVID-19 virus. “It’s like a wildfire. You can’t always wait until you collect data to make decisions — having a model can help fill this void,” Poor said.

 “Hopefully, this model could give leaders another tool to better understand the reasons why, for example, the COVID-19 virus is spreading so much more rapidly than predicted, and thereby help them deploy more effective and timely countermeasures,” Poor said.


Bibliography:

Rashad Eletreby, Yong Zhuang, Kathleen M. Carley, Osman YaฤŸan, H. Vincent Poor.

The effects of evolutionary adaptations on spreading processes in complex networks. 

Proceedings of the National Academy of Sciences, 2020; 117 (11): 5664

DOI: 10.1073/pnas.1918529117

Saturday, 21 March 2020

Study reveals how long COVID-19 remains infectious on cardboard, metal and plastic


The virus that causes COVID-19 remains for several hours to days on surfaces and in aerosols, a new study published in the New England Journal of Medicine found.

The study suggests that people may acquire the coronavirus through the air and after touching contaminated objects. Scientists discovered the virus is detectable for up to three hours in aerosols, up to four hours on copper, up to 24 hours on cardboard and up to two to three days on plastic and stainless steel.

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"This virus is quite transmissible through relatively casual contact, making this pathogen very hard to contain," said James Lloyd-Smith, a co-author of the study and a UCLA professor of ecology and evolutionary biology. "If you're touching items that someone else has recently handled, be aware they could be contaminated and wash your hands."



The study attempted to mimic the virus being deposited onto everyday surfaces in a household or hospital setting by an infected person through coughing or touching objects, for example. The scientists then investigated how long the virus remained infectious on these surfaces.

The study's authors are from UCLA, the National Institutes of Health's National Institute of Allergy and Infectious Diseases, the Centers for Disease Control and Prevention, and Princeton University. They include Amandine Gamble, a UCLA postdoctoral researcher in Lloyd-Smith's laboratory.

As shown in Panel A, the titer of aerosolized viable virus is expressed in 50% tissue-culture infectious dose (TCID50) per liter of air. Viruses were applied to copper, cardboard, stainless steel, and plastic maintained at 21 to 23°C and 40% relative humidity over 7 days. The titer of viable virus is expressed as TCID50 per milliliter of collection medium. All samples were quantified by end-point titration on Vero E6 cells. Plots show the means and standard errors ( bars) across three replicates. As shown in Panel B, regression plots indicate the predicted decay of virus titer over time; the titer is plotted on a logarithmic scale. Points show measured titers and are slightly jittered (i.e., they show small rapid variations in the amplitude or timing of a waveform arising from fluctuations) along the time axis to avoid overplotting. Lines are random draws from the joint posterior distribution of the exponential decay rate (negative of the slope) and intercept (initial virus titer) to show the range of possible decay patterns for each experimental condition. There were 150 lines per panel, including 50 lines from each plotted replicate. As shown in Panel C, violin plots indicate posterior distribution for the half-life of viable virus based on the estimated exponential decay rates of the virus titer. The dots indicate the posterior median estimates, and the black lines indicate a 95% credible interval. Experimental conditions are ordered according to the posterior median half-life of SARS-CoV-2. The dashed lines indicate the limit of detection, which was 3.33×100.5 TCID50 per liter of air for aerosols, 100.5 TCID50 per milliliter of medium for plastic, steel, and cardboard, and 101.5 TCID50 per milliliter of medium for copper.


In February, Lloyd-Smith and colleagues reported in the journal eLife that screening travelers for COVID-19 is not very effective. People infected with the virus -- officially named SARS-CoV-2 -- may be spreading the virus without knowing they have it or before symptoms appear. Lloyd-Smith said the biology and epidemiology of the virus make infection extremely difficult to detect in its early stages because the majority of cases show no symptoms for five days or longer after exposure.

"Many people won't have developed symptoms yet," Lloyd-Smith said. "Based on our earlier analysis of flu pandemic data, many people may not choose to disclose if they do know."

The new study supports guidance from public health professionals to slow the spread of COVID-19:



  • Avoid close contact with people who are sick.

  • Avoid touching your eyes, nose and mouth.

  • Stay home when you are sick.

  • Cover coughs or sneezes with a tissue, and dispose of the tissue in the trash.

  • Clean and disinfect frequently touched objects and surfaces using a household cleaning spray or wipe.


Bibliography:

Aerosol and Surface Stability of SARS-CoV-2 as Compared with SARS-CoV-1.

Neeltje van Doremalen, Trenton Bushmaker, Dylan H. Morris, Myndi G. Holbrook, Amandine Gamble, Brandi N. Williamson, Azaibi Tamin, Jennifer L. Harcourt, Natalie J. Thornburg, Susan I. Gerber, James O. Lloyd-Smith, Emmie de Wit, Vincent J. Munster.

New England Journal of Medicine, 2020;

DOI: 10.1056/NEJMc2004973

Friday, 20 March 2020

Coronavirus spreads quickly and sometimes before people have symptoms, study finds


Infectious disease researchers at The University of Texas at Austin studying the novel coronavirus were able to identify how quickly the virus can spread, a factor that may help public health officials in their efforts at containment. They found that time between cases in a chain of transmission is less than a week and that more than 10% of patients are infected by somebody who has the virus but does not yet have symptoms.

In the paper in press with the journal Emerging Infectious Diseases, a team of scientists from the United States, France, China and Hong Kong were able to calculate what's called the serial interval of the virus. To measure serial interval, scientists look at the time it takes for symptoms to appear in two people with the virus: the person who infects another, and the infected second person.

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Researchers found that the average serial interval for the novel coronavirus in China was approximately four days. This also is among the first studies to estimate the rate of asymptomatic transmission.

The speed of an epidemic depends on two things -- how many people each case infects and how long it takes for infection between people to spread. The first quantity is called the reproduction number; the second is the serial interval. The short serial interval of COVID-19 means emerging outbreaks will grow quickly and could be difficult to stop, the researchers said.

"Ebola, with a serial interval of several weeks, is much easier to contain than influenza, with a serial interval of only a few days. Public health responders to Ebola outbreaks have much more time to identify and isolate cases before they infect others," said Lauren Ancel Meyers, a professor of integrative biology at UT Austin. "The data suggest that this coronavirus may spread like the flu. That means we need to move quickly and aggressively to curb the emerging threat."



Meyers and her team examined more than 450 infection case reports from 93 cities in China and found the strongest evidence yet that people without symptoms must be transmitting the virus, known as pre-symptomatic transmission. According to the paper, more than 1 in 10 infections were from people who had the virus but did not yet feel sick.

Previously, researchers had some uncertainty about asymptomatic transmission with the coronavirus. This new evidence could provide guidance to public health officials on how to contain the spread of the disease.

"This provides evidence that extensive control measures including isolation, quarantine, school closures, travel restrictions and cancellation of mass gatherings may be warranted," Meyers said. "Asymptomatic transmission definitely makes containment more difficult."

Meyers pointed out that with hundreds of new cases emerging around the world every day, the data may offer a different picture over time. Infection case reports are based on people's memories of where they went and whom they had contact with. If health officials move quickly to isolate patients, that may also skew the data.

"Our findings are corroborated by instances of silent transmission and rising case counts in hundreds of cities worldwide," Meyers said. "This tells us that COVID-19 outbreaks can be elusive and require extreme measures."

Zhanwei Du of The University of Texas at Austin, Lin Wang of the Institut Pasteur in Paris, Xiaoke Xu of Dalian Minzu University, Ye Wu of Beijing Normal University and Benjamin J. Cowling of Hong Kong University also contributed to the research. Lauren Ancel Meyers holds the Denton A. Cooley Centennial Professorship in Zoology at The University of Texas at Austin.



The research was funded by the U.S. National Institutes of Health and the National Natural Science Foundation of China.


Bibliography:

Serial Interval of COVID-19 from Publicly Reported Confirmed Cases.

Zhanwei Du, Xiaoke Xu, Ye Wu, Lin Wang, Benjamin J. Cowling, Lauren Ancel Meyers.

Emerging Infectious Diseases, April 2020;

DOI: 10.3201/eid2606.200357

Saturday, 14 March 2020

COVID-19: Should I be tested? What you need to know about these precious tests


Governments around the world are fighting to contain and slow the rapid spread of the new coronavirus (137,445 infections and 5,088 deaths as of March 13). During this critical phase of the pandemic, social restrictions, confinement and screening tests are at the heart of the efforts.

Who should get tested?

Currently, there are two main cases for which a coronavirus screening test should be carried out: showing symptoms and / or having been in contact with an infected person.

The main symptoms of COVID-19, the disease caused by the coronavirus SARS-CoV-2, are: fever, dry cough and shortness of breath. These symptoms are very similar to those of the flu, so you need the advice of a doctor to determine if testing for the virus is necessary.

Local spread, sometimes without apparent signs…
Initially, the Centers for Disease Control and Prevention (CDC) recommended testing only people with symptoms who have been potentially exposed to the virus. However, to the surprise of public health officials, several of the first cases in the United States as well as in other countries, having tested positive for the virus, had no obvious exposure.

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This development therefore suggests that the virus is transmitted locally, which means that it spreads easily from one person to another and / or that individuals may have transmitted the virus without experiencing obvious symptoms.

In response, on March 4, 2020, the CDC changed their recommendations to allow anyone with symptoms similar to COVID-19 to be tested as long as a doctor approves the request. Since the number of tests available is limited, the CDC encourages physicians to minimize unnecessary tests and to consider the risks of exposure to a patient before ordering them.

Screening is important because it quarantines infected patients and stops the spread of the virus.

As of this writing, there is no specific drug, vaccine, or treatment available for COVID-19, but that does not mean that screening tests are unnecessary. On the contrary, it allows you to define which patients are actually infected so that they can be quarantined in order to limit the spread of the virus.

Another advantage of carrying out a test is that it allows public health professionals to get a better idea of ​​the number of cases and the spread of the virus in the local or national population.



What does the test look like?

For a patient, the virus screening process is simple and can potentially take place almost anywhere: it usually involves collecting a swab deep into the nasal cavity to collect cells from the back of the nose.

The sample is then sent to a laboratory where it will be tested to determine whether the patient's cells are infected with the virus or not. The same process is used to take a sample for the flu test.

How does the screening test work?

Although collecting a sample is easy, it is much more complicated to determine whether or not a person is infected with SARS-CoV-2. In fact, the current method consists in looking for the genetic material of the virus (ie RNA) in the cells of a patient.

In order to detect the presence of RNA, laboratories perform a procedure called reverse transcription polymerase chain reaction. This method consists first of converting any viral RNA into DNA, before replicating it millions of times until there are enough copies for detection to take place.

If virus genetic material is found in the sample, then it is confirmed that the patient is infected and has SARS-CoV-2. It usually takes between 24 and 72 hours to get the results of a test.

At the start of the ramp-up of testing, accuracy raised concerns after a study found that 3% of tests in China were negative while the samples were actually positive. But this type of genetic test is generally very accurate (more than rapid flu tests), and the health benefits of the test outweigh the risk of error.



Are there enough tests?

The availability of tests can indeed be a problem. You should know that the latter requires a kit: either specialized equipment and personnel trained accordingly.

Integrated DNA Technologies, a company collaborating with the CDC, shipped 700,000 tests to commercial, university and health laboratories on March 6 in the United States. Quest Diagnostics and LabCorp, two large commercial test manufacturers, have started manufacturing their own test kits, available since March 9.

Many companies, hospitals and other institutions are now fighting to develop more tests to diagnose COVID-19. On March 10, 2020, Alex Azar, Secretary of Health and Social Services, announced that 2.1 million test kits are now available, of which more than one million have been shipped to certified laboratories. Millions more are expected to ship this week.

Will all potential patients have to be tested?

Realistically, it is technically impossible to test all people potentially affected by COVID-19. Therefore, most health officials believe it is important to prioritize screening for those who need it most, those at high risk: those over the age of 65, immunocompromised, those with other diseases (heart disease, lung disease, diabetes), individuals who have been in close contact with infected patients as well as those showing symptoms and having traveled to areas with high rates of infection.

As more tests become available, more people will be able to be tested.

There is also a need to develop faster tests, which do not require special equipment and personnel. Namely, these tests allow experts to better understand the progression of the epidemic and try to predict the impact of the virus on society.

Much remains to be learned about this new coronavirus…

One day, this pandemic will end. However, in the meantime, the population must absolutely take care to respect the measures imposed, in particular the fact of washing their hands correctly and regularly, coughing in the crook of the elbow and trying to minimize the risk of exposure and / or transmission of the virus to other people by limiting social activities.




There is still a lot to learn about this new coronavirus, and only time will tell if it will disappear from the human population (as SARS did in 2004) or if it will become, like the flu, a seasonal disease.

Source

Monday, 9 March 2020

Researchers created new type of mouth-dissolving vaccine


In the midst of the SARS-CoV-2 coronavirus epidemic, immunologists are working harder to develop an effective vaccine as quickly as possible. Once developed, this vaccine must be produced, packaged and distributed worldwide so that it can be administered to populations. However, a vaccination campaign is not without its pitfalls: it is necessary to make suitable bottles, store the vaccines in refrigerated containers, produce hundreds of thousands of needles, etc. These prerequisites are time consuming and costly. This is why a team of researchers has recently developed a whole new type of vaccination, taking the form of a small film dissolving in the mouth. The vaccine film, fast and very inexpensive to produce, does not require any needle or refrigerated storage.

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The research group has developed a novel method to stabilize live viruses and other biological medicines in a rapidly dissolving film that does not require refrigeration and can be given by mouth. Since the ingredients to make the film are inexpensive and the process is relatively simple, it could make vaccine campaigns much more affordable. Large quantities could be shipped and distributed easily given its flat, space saving shape.

Globally, vaccination rates have improved over the past decade, but are still too low – 13.5 million children were not vaccinated in 2018. This new technology, recently published in the journal Science Advances, has the potential to dramatically improve global access to vaccines and other biological medicines.



A technique inspired by hard candy

The research team began developing this technology in 2007, when the National Institutes of Health asked us to develop a needle-free, shelf-stable delivery method for a vaccine.

The idea of developing a film was inspired by a documentary about how the DNA of insects and other living things can be preserved for millions of years in amber. This got them into thinking about hard candy.

It was a simple idea, yet no one had tried it. So they went to work mixing a variety of formulations containing natural ingredients like sugars and salts and testing them for their ability to form a solid amber-like candy.

The vaccine film created by the researchers is simple and inexpensive to produce. In addition, it can be stored at room temperature. Credit: Maria Croyle


Initially, many of the preparations they tested either killed the organism as the film formed or crystallized during storage, shredding the virus or the bacteria they were trying to preserve.

But finally, after about 450 tries over the course of a year, they found a formulation that could suspend viruses and bacteria in a peelable film.

As they gained more experience with the production process, they worked to simplify it so extensive technical training would not be needed to make it. Additionally, they tweaked the ingredients so they would dry faster, enabling one to make a batch of vaccine in the morning and ship it after lunch.

All stored vaccines lose their potency over time. The rate at which they do so mostly depends on the temperature at which they are kept. Keeping vaccines continuously refrigerated is difficult and expensive – and in some parts of the world, nearly impossible. So creating a vaccine that can be stored and transported at room temperature is a huge advantage.

Vaccine films: they keep viruses stable and are easy to administer

The biggest breakthrough in this project came when the researchers finished their work on the Ebola vaccine and found films containing the virus made three years ago, stored in a sealed container on the laboratory bench. On a whim, they rehydrated and tested them to determine if the vaccine was still capable of inducing an immune response. Over 95% of the viruses in the film were still active. Achieving this type of shelf life for an unrefrigerated vaccine was amazing.

Structure of the vaccine film. Credits: Irnela Bajrovic et al. 2020

The ecological footprint left by global immunization campaigns is not often considered. The 2004 Philippine Measles Elimination Campaign, which immunized 18 million children in one month, generated 19.5 million syringes, or 143 tons of sharps waste and nearly 80 tons of nonhazardous waste – empty vials, syringe wrappers, caps, cotton swabs and packaging. The implications for a larger campaign are significant.

“Our film, by contrast, can be distributed by health workers equipped with only an envelope containing the vaccine. Once taken, it will leave no trace, except for a healthy global population.” the author said.




Bibliography:

Novel technology for storage and distribution of live vaccines and other biological medicines at ambient temperature

Irnela Bajrovic, Stephen C. Schafer, Dwight K. Romanovicz and Maria A. Croyle

Science Advances  04 Mar 2020:
Vol. 6, no. 10, eaau4819

DOI: 10.1126/sciadv.aau4819

Saturday, 7 March 2020

What Really Works to Keep The Coronavirus Away?



The World Health Organization has declared that COVID-19, the disease caused by the new coronavirus, has a higher fatality rate than the flu. As of March 4, 2020, nine deaths have been reported in the U.S. Brian Labus, a professor of public health, provides essential safety information for you, from disinfectants to storing food and supplies.

1. What can I do to prevent becoming infected?

When people are sick with a respiratory disease like COVID-19, they cough or sneeze particles into the air. If someone is coughing near you, the virus could easily land on your eyes, nose or mouth. These particles travel only about six feet and fall out of the air rather quickly. However, they do land on surfaces that you touch all the time, such as railings, doorknobs, elevator buttons or subway poles. The average person also touches their face 23 times per hour, and about half of these touches are to the mouth, eyes, and nose, which are the mucosal surfaces that the COVID-19 virus infects.

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We public health professionals can’t stress this enough: Proper hand-washing is the best thing you can do to protect yourself from a number of diseases including COVID-19. While hand-washing is preferred, hand sanitizers with at least a 60% alcohol concentration can be an effective alternative to always using soap and water, but only if your hands are not visibly soiled.


2. Wouldn’t it be easier just to clean surfaces?

Not really. Public health experts don’t fully understand the role these surfaces play in the transmission of disease, and you could still be infected by a virus that landed directly on you. We also don’t know how long the coronavirus that causes COVID-19 can survive on hard surfaces, although other coronaviruses can survive for up to nine days on hard surfaces like stair railings.

Frequent cleaning could remove the virus if a surface has been contaminated by a sick person, such as when someone in your household is sick. In these situations, it is important to use a disinfectant that is thought to be effective against the COVID-19 virus. Although specific products have not yet been tested against COVID-19 coronavirus, there are many products that are effective against the general family of coronaviruses. Cleaning recommendations using “natural” products like vinegar are popular on social media, but there is no evidence that they are effective against coronavirus.



You also have to use these products properly in accordance with the directions, and that typically means keeping the surface wet with the product for a period of time, often several minutes. Simply wiping the surface down with a product is usually not enough to kill the virus.

In short, it isn’t possible to properly clean every surface you touch throughout your day, so hand-washing is still your best defense against COVID-19.

3. What about wearing masks?

While people have turned to masks as protection against COVID-19, masks often provide nothing more than a false sense of security to the wearer. The masks that were widely available at pharmacies, big-box stores and home improvement stores – until a worried public bought them all – work well at filtering out large particles like dust. The problem is that the particles that carry the COVID-19 virus are small and easily move right through dust masks and surgical masks. These masks may provide some protection to other people if you wear one while you are sick – like coughing into a tissue – but they will do little to protect you from other sick people.

N95 masks, which filter out 95% of the small, virus-containing particles, are worn in health care settings to protect doctors and nurses from exposure to respiratory diseases. These masks provide protection only if they are worn properly. They require special testing to ensure that they provide a seal around your face and that air doesn’t leak in the sides, defeating the purpose of the mask. People wearing the mask also must take special steps when removing the mask to ensure that they are not contaminating themselves with the viral particles that the mask filtered out. If you don’t wear the mask properly, don’t remove it properly or put it in your pocket and reuse it later, even the best mask won’t do you any good.



4. Should I stockpile food and supplies?

As a general preparedness step, you should have a three-day supply of food and water in case of emergencies. This helps protect from disruptions to the water supply or during power outages.

While this is great general preparation advice, it doesn’t help you during a disease outbreak. There is no reason to expect COVID-19 to cause the same damage to our infrastructure that we Americans would see after an earthquake, hurricane or tornado, so you shouldn’t plan for it in the same way. While you don’t want to run out of toilet paper, there is no reason to buy 50 packages.

A Wuhan-type quarantine is extremely unlikely, as a quarantine won’t stop the spread of a disease that has been found all over the world. The types of disruptions that you should plan for are small disruptions in your day-to-day life. You should have a plan in case you or a family member gets sick and you can’t leave the house for a few days. This includes stocking up on basic things you need to take care of yourself, like food and medicines.



If you do get sick, the last thing you are going to want to do is run to the grocery store, where you would expose other people to your illness. You shouldn’t wait until you are out of an important medication before requesting a refill just in case your pharmacy closes for a couple days because all their employees are sick. You also should plan for how to handle issues like temporary school or day care closures. You don’t need to prepare anything extreme; a little common-sense preparation will go a long way to make your life easier if you or your loved ones become sick.

Source

Saturday, 29 February 2020

New stem cell procedure cured mice with diabetes


Stem cell therapies have been studied for many years by biologists, as their therapeutic potential for various diseases is great. This is especially the case with diabetes, where the differentiation of stem cells into insulin-secreting pancreatic beta cells could help stabilize or even reverse the disease. Recently, a team of researchers made a new breakthrough in the field: pluripotent stem cells differentiated into pancreatic beta cells made it possible to quickly cure mice suffering from diabetes. Although the results are not yet applicable to humans, they remain extremely promising.

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In a study, researchers figured out a new way to coax human pluripotent stem cells (hPSCs) into pancreatic beta cells that make insulin. When these insulin-producing cells were transplanted into mice induced to have an acute form of diabetes, their condition was rapidly cured.

“These mice had very severe diabetes with blood sugar readings of more than 500 milligrams per deciliter of blood — levels that could be fatal for a person — and when we gave the mice the insulin-secreting cells, within two weeks their blood glucose levels had returned to normal and stayed that way for many months,” said principal investigator Jeffrey R. Millman, PhD, an assistant professor of medicine and of biomedical engineering at Washington University.



Transform pluripotent stem cells into pancreatic beta cells

Pluripotent stem cells are essentially blank, undifferentiated cells with the ability to grow into other kinds of cells that exist all throughout the body. Harnessing that potential, in the diabetic context, means researchers could devise ways of tweaking stem cells to become the insulin-producing cells that diabetics lack, helping them to control high blood sugar and stay healthy.

Protocol for differentiating pluripotent stem cells into pancreatic beta cells used by researchers. Credits: Nathaniel J. Hogrebe et al. 2020


Scientists have been investigating how to do this for years, reporting a number of incremental successes in animal models as our understanding of the processes behind stem cell manipulation increases.

Millman's lab has been busy too. In 2016, they devised a way to produce insulin-secreting cells – derived from patients with type 1 diabetes – that functioned in response to glucose. A few years later, they learned how to augment the level of insulin secretion in stem-cell-derived pancreatic beta cells.

Better master the differentiation of pluripotent stem cells

Now, the researchers have shown a new technique they developed can more efficiently convert human stem cells into insulin-producing cells that more effectively control blood sugar.

“A common problem when you’re trying to transform a human stem cell into an insulin-producing beta cell — or a neuron or a heart cell —is that you also produce other cells that you don’t want,” Millman said. “In the case of beta cells, we might get other types of pancreas cells or liver cells.”

Off-target pancreas and liver cells don’t hurt anything when implanted into a mouse, but they don’t fight diabetes either.

However, a new technique now looks like it can keep cell differentiation on target. In the new study, the team found that transcription factors that drive stem cells towards becoming pancreatic cells are linked to the state of the cell's cytoskeleton, a support structure inside cells that acts as a kind of skeleton, made up of microfilaments of various protein fibres.

Actin: it plays a key role in cell differentiation

One of these proteins is called actin, which plays an important role in cellular function, and, it turns out, cell differentiation as well.

"We found that manipulating cell–biomaterial interactions and the state of the actin cytoskeleton altered the timing of endocrine transcription factor expression and the ability of pancreatic progenitors to differentiate into stem-cell-derived beta cells," the authors explain in their paper.

Actin, a cytoskeleton protein, plays a key role in cell differentiation. It is present in two forms: as an actin monomer (actin G, high) and as an actin filament (actin F, low). Credit: Thomas Splettstoesser

"We were able to make more beta cells, and those cells functioned better in the mice, some of which remained cured for more than a year," Millman explains; control animals, who were not given the cell transplants, ended up dying, such was the severity of their induced diabetes.

That's not all. The same cytoskeletal manipulations also showed potential to better control the differentiation of other kinds of cells, including liver, oesophagus, stomach, and intestine cells, the researchers say. If so, the technique might enhance stem cell treatments for other kinds of pathologies, not just diabetes.



He explained that there still is much to do before this strategy can be used to treat people with diabetes. They will need to test the cells over longer periods of time in larger animal models and work to automate the process to have any hope of producing beta cells that can help the millions of people who currently require insulin injections to control their diabetes. But the research is continuing.


Bibliography:

Targeting the cytoskeleton to direct pancreatic differentiation of human pluripotent stem cells.

Hogrebe NJ, Augsornworawat P, Maxwell KG, Velazco-Cruz L, Millman JR

Nature Biotechnology

https://doi.org/10.1038/s41587-020-0430-6

Thursday, 27 February 2020

Coronavirus: US begins trial of Gilead's remdesivir in Covid-19 patients


A clinical trial to evaluate the safety and efficacy of the experimental antiviral Remdesivir in hospitalized adults diagnosed with COVID-19, has started at the University of Nebraska Medical Center (UNMC). The trial director is the National Institute of Allergies and Infectious Diseases (NIAID), which is part of the National Institutes of Health (NIH). It is the first clinical trial in the United States to evaluate an experimental treatment for COVID-19.

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The first participant in the trial is an American who was repatriated after being quarantined on the cruise ship Diamond Princess , which docked in Yokohama, Japan, and volunteered to participate in the study. The research can be adapted to assess additional investigative treatments and to enroll participants at other sites in the United States and around the world.

The need to develop a rapid treatment for COVID-19

There is no specific therapeutic treatment approved by the Food and Drug Administration (FDA) to treat people with COVID-19. The infection can cause mild to severe respiratory illness, and symptoms may include fever, cough, and shortness of breath. As of February 24, the World Health Organization (WHO) had reported 77,262 confirmed cases of COVID-19 and 2,595 deaths in China, as well as 2,069 cases and 23 deaths in 29 other countries.



According to the Centers for Disease Control and Prevention (CDC), 14 confirmed cases of COVID-19 have been reported in the United States and another 39 cases among people repatriated to the United States.

Remdesivir, developed by Gilead Sciences Inc., is an experimental broad-spectrum antiviral treatment. It has already been tested in humans against the Ebola virus and has shown promise in animal models for the treatment of Middle Eastern Respiratory Syndrome (MERS) and Severe Acute Respiratory Syndrome (SARS). Clinical trials of remdesivir are also underway in China.

Remdesivir: a double-blind human clinical trial

All potential participants will undergo a basic physical exam before receiving treatment. Eligible study participants will then be randomly assigned to either the experimental treatment group or the placebo group. The study is double-blind, which means that trial investigators and participants do not know who is receiving Remdesivir or a placebo.

Chemical structure of the broad-spectrum antiviral remdesivir. Credit: Gilead

Participants in the experimental treatment group will receive 200 milligrams (mg) of intravenous remdesivir on the first day of study enrollment. They will receive another 100 mg per day for the duration of hospitalization, for a maximum of 10 days. The placebo group will receive, at equal volume, a solution that resembles remdesivir but contains only inactive ingredients.

Clinicians will regularly monitor participants and assign them daily scores based on a predefined scale of clinical outcomes, which takes into account factors such as temperature, blood pressure and the use of supplemental oxygen, among other things. Participants will also be asked to provide blood samples and swabs from the nose and throat approximately every two days. Researchers will test these specimens for SARS-CoV-2.



Initially, the investigators will compare the results of participants on day 15 in the remdesivir group and the placebo group to see if the investigational drug increased clinical benefit compared to placebo. Results are scored on a seven-point scale from full recovery to death. Investigators will reassess this scale after examining the data from the first 100 participants.

Source (NIH)

Sunday, 23 February 2020

A powerful antibiotic discovered thanks to the artificial intelligence


A powerful antibiotic was discovered for the very first time thanks to machine learning (literally “machine learning”), a field of study of artificial intelligence which is based on mathematical and statistical approaches to give computers the ability to learn from data, that is, to improve their performance in solving tasks without being explicitly programmed for them.

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Now, thanks to artificial intelligence , a team from the Massachusetts Institute of Technology (MIT) claims that halicin (the powerful antibiotic in question) kills some of the most dangerous strains of drug-resistant bacteria in the world.

This drug works differently from existing antibacterials and is the first of its kind to be discovered by AI browsing large digital libraries of pharmaceutical compounds.



Tests by researchers have shown that the drug successfully eliminates a range of antibiotic-resistant bacteria strains, including Acinetobacter baumannii and Enterobacteriaceae, two of the three pathogens to be given high priority and that the World Health Organization Health (WHO) also classifies as "critical".

The culture plate on the right contains bacteria resistant to all the antibiotics tested so far. Credit: Science History Images / Alamy

"In terms of antibiotic discovery, this is absolutely a first," said Regina Barzilay, project lead researcher and machine learning specialist at MIT. "I think it's one of the most powerful antibiotics discovered to date," added James Collins, a bioengineer on the MIT team. "It has remarkable activity against a wide range of pathogens resistant to current antibiotics."

Be aware that antibiotic resistance occurs when bacteria mutate and evolve to bypass the mechanisms that antimicrobial drugs use to kill them. Experts say that without new antibiotics to fight resistance, 10 million lives around the world could be threatened by infections each year by 2050.

AI to discover potential new antibiotics

In order to discover new antibiotics, the researchers first trained a “deep learning” algorithm to identify the types of molecules that kill bacteria. To do this, Scientists trained it to analyse the structure of 2,500 drugs and other compounds to find those with the most anti-bacterial qualities that could kill E. coli.

Once the algorithm learned which molecular features make good antibiotics, scientists let it browse a library of more than 6,000 compounds being studied to treat various human diseases.

And, rather than looking for potential antimicrobials, the algorithm focused on compounds that seemed effective, but were different from existing antibiotics. Therefore increased the chances that these drugs will act in a radically new way and that bacteria have not yet developed resistance to them.

Jonathan Stokes, the first author of the study, said it took a matter of hours for the algorithm to assess the compounds and come up with some promising antibiotics. One, which the researchers named “halicin” after Hal, the astronaut-bothering AI in the film 2001: A Space Odyssey, looked particularly potent.

Very promising positive results!

Since this discovery, researchers have been able to treat many drug-resistant infections with halicin, a compound that was originally developed to treat diabetes, but which ultimately did not work. Tests on bacteria collected from patients have shown that halicin can eradicate Mycobacterium tuberculosis , the bacteria responsible for tuberculosis, as well as strains of enterobacteriaceae resistant to carbapenems, a group of antibiotics considered to be the last resort for such infections.

Halicin has also successfully eliminated difficult infections and multidrug-resistant Acinetobacter baumannii infections in mice. To research new drugs, the team then turned to a large digital database of around 1.5 billion compounds. They adjusted the algorithm so that the latter analyzes 107 million of these compounds. Then, three days later, the program returned a shortlist of 23 potential antibiotics, two of which appear to be particularly potent.

Use AI to find other more targeted antibiotics

Now scientists plan to search more databases for potential antibiotics. Stokes stated that it would have been impossible to screen all of the compounds by conventional means of obtaining or manufacturing the substances, and then to test them in the laboratory. "Being able to perform these experiments on a computer greatly reduces the time and cost of examining these compounds," he said.

Barzilay now wants to use the algorithm to find more selective antibiotics in the bacteria they kill. This would mean that taking the antibiotic would kill only the bacteria causing an infection, and not also all the healthy bacteria that live in the gut in particular.

Even more ambitious, scientists aim to use the algorithm to design powerful new antibiotics from scratch. "This work is truly remarkable," said Jacob Durrant, who works on computer-aided drug design at the University of Pittsburgh. “Their approach highlights the power of computer-aided drug discovery. It would be impossible to physically test 100 million compounds to determine antibiotic activity.”



Indeed, if we take into account all the typical costs of drug development, in terms of time and money, any method that can accelerate discovery, as is the case here thanks to artificial intelligence, has the potential to have a very significant impact.


Bibliography:

A Deep Learning Approach to Antibiotic Discovery

Jonathan M. Stokes, Kevin YangKyle Swanson, Wengong Jin, Andres Cubillos-Ruiz, Nina M. Donghia, Craig R. MacNair, Shawn French, Lindsey A. Carfrae, Zohar Bloom-Ackerman, Victoria M. Tran, Anush Chiappino-Pepe, Ahmed H. Badran, Ian W. Andrews, Emma J. Chory, George M. Church, Eric D. Brown, Tommi S. Jaakkola, Regina Barzilay, James J. Collins

VOLUME 180, ISSUE 4, P688-702.E13,

https://doi.org/10.1016/j.cell.2020.01.021

Friday, 21 February 2020

A woman cured of cancer gives birth to a baby from a 5 year old frozen egg


In many cases, chemotherapy treatments leave patients sterile or with reproductive disorders. Typically, doctors suggest that patients take eggs before treatment, then ripen them in vitro and freeze them for later use. Until now, no pregnancy had been able to be triggered via this process, the failures being systematic. But as part of a world first woman cured of cancer successfully carried out a pregnancy triggered via a frozen egg several years earlier. A success of a team of French researchers considered it  as a real medical breakthrough by the scientific community.

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A woman made sterile by cancer treatment gave birth after one of her immature eggs was matured, frozen and - five years later - thawed and fertilized. The study, published in the journal Annals of Oncology, describes how the baby was born to a 34-year-old French woman who had been treated with chemotherapy for breast cancer.



In vitro maturation and freezing: functional eggs several years later

Before treatment started, doctors removed seven immature eggs from her ovaries and used a technique called in vitro maturation (IVM) to allow the eggs to develop further in the laboratory. To date, there have been no successful pregnancies in cancer patients with eggs who have undergone IVM and freezing. However, some children were born following an IVM immediately followed by fertilization and transfer to the patient.

Professor Michaรซl Grynberg, head of the Department of Reproductive Medicine and Fertility Preservation at the Antoine Bรฉclรจre University Hospital, near Paris, France, is the first author of the letter.

“I saw the 29-year-old patient following her diagnosis of cancer and provided fertility counselling. I offered her the option of egg freezing after IVM and also freezing ovarian tissue. She rejected the second option, which was considered too invasive a couple of days after cancer diagnosis.”

Infographic describing the procedure used by doctors. Credits: M. Grynberg et al. 2020

Cryopreservation of ovarian tissue is an experimental method in which the outer layer of an ovary - which contains immature eggs - is removed from the body and frozen for future use. In the case of the French patient, the ultrasound revealed that there were 17 small bags filled with liquid containing immature eggs in her ovaries. But using hormones to stimulate the ovaries and ripen the eggs would have taken too long and could have made her cancer worse, leaving the recovery of immature eggs and freezing as the best option.

Towards an optimized and less invasive in vitro fertilization procedure

After five years, the patient had recovered from breast cancer but found the chemotherapy had made her infertile as she had been unable to conceive within a year. Stimulating her ovaries to prompt them to produce more eggs ran the risk that the hormones used could cause the breast cancer to recur, so she and her doctors decided to use her frozen eggs. All six eggs survived the thawing process and they were fertilised using ICSI (intracytoplasmic sperm injection); five fertilised successfully and one embryo was transferred to the patient’s womb. She became pregnant and nine months later she gave birth to a healthy baby boy called Jules on 6 July 2019.

Prof Grynberg said: “We were delighted that the patient became pregnant without any difficulty and successfully delivered a healthy baby at term. My team and I trusted that IVM could work when ovarian stimulation was not feasible. Therefore, we have accumulated lots of eggs that have been vitrified following IVM for cancer patients and we expected to be the first team to achieve a live birth this way. We continue offering IVM to our patients in combination with ovarian tissue cryopreservation when ovarian stimulation cannot be considered. This success represents a breakthrough in the field of fertility preservation.”



He concluded: “Fertility preservation should always be considered as part of the treatment for young cancer patients. Egg or embryo vitrification after ovarian stimulation is still the most established and efficient option. However, for some patients, ovarian stimulation isn’t feasible due to the need for urgent cancer treatment or some other contraindication. In these situations, freezing ovarian tissue is an option but requires a laparoscopic procedure and, in addition, in some diseases it runs the risk of re-introducing malignant cells when the tissue is transplanted back into the patient.


Bibliography:

First birth achieved after fertility preservation using vitrification of in vitro matured oocytes in a woman with breast cancer’ by M Grynberg et al. was published in Annals of Oncology at 00:01 UK time on Wednesday 19th February.

DOI: https://doi.org/10.1016/j.annonc.2020.01.005

Thursday, 20 February 2020

Coronavirus protein has just been mapped, paving the way for a vaccine



The “tip” protein of the coronavirus has just been mapped, potentially paving the way for the development of a vaccine. In fact, it is this protein that the virus uses to infect human cells.

Scientists around the world are currently doing everything they can to develop vaccines and potential drugs to fight the new coronavirus, now known as SARS-CoV-2 (SARS-CoV- 2 in French).

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We remind you that from now on, the name Covid-19 must be used to speak of the current epidemic (the disease) and that the coronavirus itself must be called SARS-CoV-2, a very scientific qualifier in which "CoV" means "coronavirus" and "SARS" (or SARS in French) is an acronym for "severe acute respiratory syndrome". Therefore, the name "SARS-CoV-2" was chosen by the International Committee on Taxonomy of Viruses to make it clear that this coronavirus is from the same family as SARS-CoV, which is at the origin of the epidemic of SARS between 2002 and 2003, which killed 774 people worldwide, including 349 in mainland China.

But now a group of researchers has discovered the molecular structure of a key protein that the coronavirus uses to invade human cells, potentially opening the door for vaccine development, according to new findings.



Discovery of a so-called “cutting-edge” protein that could be a game-changer

Previous research has shown that coronaviruses invade cells through so-called “spiked” proteins, but these proteins take different forms in different coronaviruses. Therefore, "determining the shape of the peak protein in SARS-Cov-2 is the key to determining how to target the virus," said Jason McLellan, lead author of the study and associate professor of molecular biosciences at the University of Texas at Austin.

Although the coronavirus uses many different proteins to replicate and invade human cells, the spike protein is the main surface protein it uses to bind to a receptor (another protein that acts as a gateway to a human cell). Then, after the virus protein binds to the human cell receptor, the viral membrane fuses with the human cell membrane, allowing the genome of the virus to enter human cells and begin infection.

Because of this, "if we can prevent attachment and fusion, we can prevent entry," said McLellan. But of course, to target this protein, you must already know what it looks like.

In pictures, on an atomic scale, the molecular structure of the “tip” of the SARS-2-CoV protein that the virus uses to invade human cells. Credits: Jason McLellan / University of Texas at Austin

Earlier this month, researchers released the SARS-Cov-2 genome. And it was by using this genome that McLellan and his team, in collaboration with the National Institutes of Health (NIH), identified the specific genes that encode the advanced protein. They then passed this information on to a company that created genes and sent them back. The group then injected the latter into mammalian cells in a laboratory box, and these cells then produced the peak proteins.

Then, using a very detailed microscopy technique called cryogenic electron microscopy, the group created a real three-dimensional “map” of the proteins in question.

The plan revealed the structure of the molecule, mapping the location of each of its atoms in space. "It is impressive that these researchers were able to get the structure so quickly," said Aubree Gordon, associate professor of epidemiology at the University of Michigan, who was not part of the study. "This is a very important step forward that could help in the development of a vaccine against SARS-COV-2," added Gordon.

Stephen Morse, a professor at Columbia University's Mailman School of Public Health, who was also not part of the study, also agrees. The advanced protein "would be the likely choice for the rapid development of vaccine antigens and treatments," he said. Knowing the structure of this advanced protein would indeed be "very useful for developing vaccines and antibodies with good activity, as well as the production of higher quantities of these proteins".

Towards a vaccine or a treatment to fight against the coronavirus

Now the researchers are sending their atomic discovery to dozens of research groups around the world, which are working to develop vaccines and drugs to target SARS-CoV-2. Meanwhile, McLellan and his team also hope to use the advanced protein map as the basis for a vaccine.

You should know that when foreign invaders such as bacteria or viruses invade the body, immune cells respond by producing proteins called antibodies. These antibodies bind to specific structures of the foreign invader, called an antigen. But producing antibodies can take time. Vaccines are dead or weakened antigens that cause the immune system to make these antibodies before the body is exposed to the virus.

Because of this, in theory, the spike protein itself "could be the vaccine or vaccine variants," said McLellan. Indeed, if we injected this vaccine with advanced proteins, "humans would make antibodies against this advanced protein, and then if they expose themselves one day to the virus, the body would already be prepared", he adds.

Mutations and changes to create an even more stable molecule

In addition, building on previous research they have done on other coronaviruses, the researchers have introduced mutations and changes to create a more stable molecule.



“The molecule looks really good; she behaves really well; the structure somehow demonstrates that the molecule is stable and confirms what we hoped for," said McLellan. "So now we and others will use the molecule we created as the basis for the vaccine antigen." Their colleagues at NIH will now test these proteins to find out how well they can trigger the production of antibodies.

Thanks to this new discovery, researchers believe that a vaccine is likely to be released within 18 to 24 months. "It's pretty quick compared to the normal development of a vaccine, which could take around 10 years ...," said McLellan. A case to follow closely.


Bibliography:

Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation

Daniel Wrapp, Nianshuang Wang, Kizzmekia S. Corbett, Jory A. Goldsmith, Ching-Lin Hsieh, Olubukola Abiona, Barney S. Graham, Jason S. McLellan

Science  19 Feb 2020:
eabb2507

DOI: 10.1126/science.abb2507

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