I am a scientist, businessman, author, and philanthropist. For nearly two decades, I was a professor at Harvard Medical School and Harvard School of Public Health where I founded two academic research departments, the Division of Biochemical Pharmacology and the Division of Human Retrovirology.
In the ongoing Omicron era, a new COVID-19 antibody could renew optimism for urgently required SARS-CoV-2 monoclonal therapies. Over the last three years, various versions of SARS-CoV-2 have mutated to bypass the neutralizing effects of monoclonal antibodies. Whenever new treatments received approval from the FDA , new variants emerged that could avoid these treatments, creating a game of cat and mouse between the virus and researchers looking for new antibody treatments.
1301B7 engages in multiple hydrogen bonds and salt bridges with the receptor-binding domain. The antibody's heavy chain contacts several critical residues found in Omicron variants, including those involved in ACE2 binding . Though the mutation in N417K results in a 20-fold decrease in affinity, 1301B7 maintains its binding to the mutated receptor-binding domain.
The research emphasizes 1301B7's promise as a strong contender for creating advanced vaccines and treatments for SARS-CoV-2 and its changing versions. Its distinct structural characteristics offer additional enhancement and refinement possibilities using protein—and glycan-focused approaches.
Covid Antibody Monoclonal Therapy Sars-Cov-2 Mutation FDA Variant Amino Acid
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