Science: Reveals the common molecular characteristics of powerful human antibodies that are powerfully neutralized with SARS-CoV-2.

!--:page title,14 (upi) -- --- In a new study, researchers from the Scripps Research Institute in the United States have found common molecular characteristics in humans and in the--- --- of a new coronavirus that causes COVID-19 disease in humans and in SARS-CoV-2they reviewed nearly 300 anti-SARS-CoV-2 antibodies found in recovered COVID-19 patients in their laboratories and other laboratories over the past few monthsthey noticed that some of these antibodies were extremely powerful in neutralizing the virus, and that some of these powerful antibodies were encoded by the same antibody gene, IGHV3-53related findings were published online July 13, 2020 in the journal Science, under the title "Rhttp-based of a shared antibody response to SARS-CoV-2"images from Science, 2020, doi:10.1126/science.abd2321the researchers used a powerful tool called X-ray crystallography to image two of the antibodies attached to the SARS-CoV-2 target sitethe resulting atomic structure details of this interaction should be useful to vaccine designers and scientists who want to develop antiviral drugs that target the same sites on SARS-CoV-2previous studies suggest that IGHV3-53 encoded antibodies are usually found in healthy people's blood, at least in small amountstherefore, these results offer hope that vaccines are used to raise the levels of these persistent antibodies in order to adequately protect people from the virus"This type of antibody is often isolated in patients with COVID-19," said Ian Wilson, apaper author and professor of structural biology at the Scripps Research Institute and chair of the Department of Integrated Structural and Computational Biologywe can now understand the structural basis of its interaction with SARS-CoV-2"This study provides important inspiration for the design of the effective COVID-19 vaccine," said professor Dennis Burton, co-author of thepaper and from the Department of Immunology and Microbiology at the Scripps Research Institute"To date, SARS-CoV-2 has infected more than 12 million people and killed more than half a million people worldwide, in addition to causing widespread socio-economic disruption and destruction,"developing an effective vaccine to stop the pandemic is now a top priority for world public health, although several potential vaccines are already in clinical trials, scientists do not fully understand the molecular characteristics of protective antibody responses in the new study, the researchers took a big step toward that goal the researchers first analyzed 294 different SARS-CoV-2 neutralizing antibodies isolated from the blood of PATIENTs with COVID-19 over the past few months antibodies are Y-shaped proteins produced in immune cells called B cells each B cell produces a specific type of antibody, or clone, encoded by a unique combination of antibody genes in the cell they found that an antibody gene called IGHV3-53 is the most common of 294 antibodies, encoding about 10 percent of them the researchers also noted that in their study, these IGHV3-53 encoded antibodies contained an abnormally short cDR H3 ring (CDR H3 loop) variant, where the CDR H3 ring is usually a key target binding element However, these antibodies are effective against SARS-CoV-2 compared to other non-IGHV3-53-encoded antibodies to produce a powerful response from the start these IGHV3-53-encoded antibodies have another characteristic: they appear to have only slightly mutated compared to the initial small circulation in healthy people's blood, suggesting that increasing their numbers is a good achievable goal for the SARS-CoV-2 vaccine normally, when the virus is activated, B cells begin to multiply, and some of their antibody genes mutate to produce new B cells, resulting in antibodies that are more suitable for binding to viral targets the more mutations required for this "affinity maturation" process, the more difficult it is to produce neutralizing antibodies in the virus, and the more difficult it is to induce the same process with a vaccine fortunately , the IGHV3-53 antibodies found in this study do not appear to have experienced or rarely experienced affinity maturation, but have been very effective in neutralizing the virus--- suggesting that the vaccine may be relatively easy to induce protective responses from these powerful neutralizing antibodies "The coronavirus has been around for hundreds to thousands of years," Wilson said we can imagine that our immune system has evolved to carry such antibodies to respond forcefully and immediately " provides important information for vaccine design and clinical trials The researchers used high-resolution X-ray crystallography to image two different IGHV3-53 antibodies that bind to targets on SARS-CoV-2 the target point, known as the receptor binding site, is a key structure in the virus's "stingy" protein, which usually binds to receptors on human cells to begin the process of cell infection many antibodies that neutralise SARS-CoV-2 appear to be achieved by blocking the virus's binding to receptors "We were able to reveal the unique structural characteristics of these IGHV3-53 encoded antibodies--- which contributed to their high affinity and specificity to the SARS-CoV-2 receptor binding site," said Dr Meng Yuan, co-lead author of the paper and a postdoctoral research assistant at Wilson Labs "These detailed atomic-level structural data should be of interest to vaccine designers and drug developers, " , the researchers said they identified IGHV3-53-encoded antibodies as key elements of an immune response to COVID-19, suggesting that the levels of these antibodies may be a marker of the success of the trial in an ongoing and future vaccine clinical trial (Bioon.com) !--/ewebeditor: !--webeditor: pagetitle"--/References: 1 Meng Yuan et al R R Basis of a shared antibody to SARS-CoV-2 Science, 2020, doi: 10.1126/science.abd2321.2 Scientists key element of the strong antibody response to COVID-19.