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Antibody binding-site conserved across COVID-19 virus variants

Deb Kelly, professor of biomedical engineering, and a team of biomedical engineers used a novel toolkit of approaches to uncover the first full structure of a SARS-CoV-2 protein, with findings that could inform advanced treatments and vaccines. Learn more about these research findings through this Penn State News story. Penn State College of Engineering “We discovered new features about the N protein structure that could have large implications in antibody testing and the long-term effects of all SARS-related pandemic viruses,” said Deb Kelly, professor of biomedical engineering (BME), Huck Chair in Molecular Biophysics and director of the Penn State Center for Structural Oncology, who led the research. “Since it appears that the N protein is conserved across the variants of SARS-CoV-2 and SARS-CoV-1, therapeutics designed to target the N protein could potentially help knock out the harsher or lasting symptoms some people experience.”

Conserved Antibody Binding-Site Identified Across COVID-19 Variants

  A Penn State research team found that the N protein on SARS-CoV-2 is conserved across all SARS-related pandemic coronaviruses (top, from left: SARS-CoV-2, civet, SARS-CoV, MERS). The protein differs from other coronaviruses, such as those that cause the common cold (bottom, from left: OC43, HKU1, NL63 and 229E). Credit: Kelly Lab/Penn State. Read Time: A tiny protein of SARS-CoV-2, the coronavirus that gives rise to COVID-19, may have big implications for future treatments, according to a team of Penn State researchers. Using a novel toolkit of approaches, the scientists uncovered the first full structure of the Nucleocapsid (N) protein and discovered how antibodies from COVID-19 patients interact with that protein. They also determined that the structure appears similar across many coronaviruses, including recent COVID-19 variants — making it an ideal target for advanced treatments and vaccines. They reported their results in Nanoscale.

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