Beaming virus

View 1 excerpt, cites background. International journal of molecular sciences. View 2 excerpts, cites background. Inactivation methods for whole influenza vaccine production. Reviews in medical virology. Journal of immunology research. Eimeria tenella oocysts attenuated by low energy electron irradiation LEEI induce protection against challenge infection in chickens. Veterinary parasitology. Materials Science, Medicine.

Human platelet lysates for human cell propagation. Comprehensive Biotechnology. Electron beam inactivation of Tulane virus on fresh produce, and mechanism of inactivation of human norovirus surrogates by electron beam irradiation. International journal of food microbiology. Highly Influential. View 5 excerpts, references background and methods. Virus inactivation studies using ion beams, electron and gamma irradiation.

Abstract Known methods of virus inactivation are based on the chemical action of some substances such as acetylethylenimine, betapropiolactone, glycidalaldehyde, formaldehyde, etc. In such a process, … Expand. View 4 excerpts, references background and methods. Kurlander said Salk in was given permission to test the vaccine on healthy children and began with his three sons, followed by a vaccination pilot study of 7, children in Pittsburgh schools.

While the results were positive, the vaccine still needed to be tested more widely to gain approval. The March of Dimes in organized a national field trial of 1. Kurlander said March was a frightening time in this country when the coronavirus spread in ways reminiscent of polio. He said it was instructive to remember what it took to nearly eradicate polio and what we could do when we work together to face a common enemy.

Unfortunately, many Americans no longer trust the medical community and the coronavirus, our common enemy, has claimed over , lives in this country. We are as far away from working together today as when the virus came calling nearly two years ago.

Jonas Salk, who developed the polio vaccine, made the cover of Time magazine on March 29, Cease-and-desist order issued for Baton Rouge insurance agent. Fort Polk welcomes Nielson as senior enlisted soldier. Email newsletter signup Sign up for our daily email newsletter. However, the SARS-CoV-2 virus's spike protein molecule—which the APS helped researchers identify as the target site of current vaccines—has been able to mutate ever so slightly and still attach itself to human cells more readily or tightly.

Depending on the degree of mutation, antibodies can then fail to recognize the mutated viruses. Ian Wilson, a scientist at the Scripps Research Institute, leads a laboratory whose APS-informed work has advanced understanding of dominant and emerging variants of the virus. They specifically narrowed their lens on the receptor binding domain RBD of the spike protein.

The RBD is a part of the virus that latches onto and invades cells to increase infection. This focus helped the Wilson lab determine crystal structures of many human antibodies combined with the RBD and see exactly how antibodies target and neutralize the virus. Ten months later, when it was reported that SARS-CoV-2 was infecting farmed mink in Denmark and that the mutated viruses were transmissible to humans, the Wilson lab built on this initial research to study the emerging variants.

They initially identified vulnerable sites on the virus surface that could be targeted by neutralizing antibodies. They also identified the more conserved sites—regions on the viral surface that are often less mutated—which, when targeted by antibodies, are effective at neutralizing the virus's emerging variants. Conserved sites of the viral surface, it turns out, are critical to study because while the virus may relentlessly change, certain regions of its spike protein cannot accommodate mutations, as they would lose essential viral function and fitness.

By changing too much, the virus wouldn't be itself anymore. Antibodies target these sites and more changeable sites with different degrees of success. Our study was able to reveal conserved regions on these different viruses that can be targeted by cross-neutralizing antibodies. In another study of the virus's escape mechanism published in Science, the Wilson lab tested a panel of 17 neutralizing antibodies isolated from COVID patients, or from mice designed to carry human cells or human genetic and physiological properties.

In these tests, two mutations of the virus in the RBD were particularly able to evade a number of neutralizing antibodies. However, when more conserved sites were tested, the variants fared less well; the antibodies were still able to target the variants.

Analysis of the antibodies that bind to these conserved regions using beamline data helps researchers identify ways to resist variants more effectively and guide next-generation vaccine and treatment design.

As detailed in Cell, Abraham studied viral sequences collected from the patient at various times during infection—from up to days after they were diagnosed with COVID He found that the immunocompromised patient's virus over time evolved to acquire RBD mutations that could fool antibodies into no longer recognizing it. When X-ray crystal structures of the antibodies were examined at the APS, it became clear that the SARS-CoV-2 spike protein can build a mature resistance to antibodies—and scientists can see exactly where it did so at a molecular level.

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