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This week, Lab.Equipment has sourced a new Biotech article published from GEN just for you:
Two human neutralizing antibodies have been isolated that bind to the glycoprotein spike of the SARS-CoV-2 virus and thereby prevent the virus from entering host cells. Although the antibodies appear capable of working alone—each binds a different epitope on the spike’s receptor binding domain (RBD)—they may work better as a team, that is, if they are administered together in an antibody “cocktail.”
The new findings come from scientists in China affiliated with the Chinese Academy of Sciences (such as the Beijing Institutes of Life Science and the Tianjin Institute of Industrial Biotechnology) and other institutions in the nation. These scientists report that the antibodies—which are called B38 and H4—were isolated from a patient who recovered from COVID-19. The scientists also present results indicating that the antibodies block the SARS-CoV-2 spike from binding to the human ACE2 receptor.
Details appeared May 13 in the journal Science, in an article entitled, “A noncompeting pair of human neutralizing antibodies block COVID-19 virus binding to its receptor ACE2.”
“A competition assay indicates their different epitopes on the RBD, making them a potential virus-targeting mAb-pair to avoid immune escape in future clinical applications,” the article’s authors wrote. “Moreover, a therapeutic study in a mouse model validated that these antibodies can reduce virus titers in infected lungs.”
The results obtained with the mouse model suggest that the antibodies may offer therapeutic benefits. To understand how these benefits are achieved, the scientists carried out a structural analysis and generated images of RBD-B38 complex. This complex, the scientists determined, reveals that “most residues on the epitope overlap with the RBD-ACE2 binding interface, explaining the blocking effect and neutralizing capacit... Want to read more? Visit the GEN – Genetic Engineering and Biotechnology News Blog.
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