Abstract
Following the initial surges of the Alpha (B.1.1.7) and the Beta (B.1.351) variants, a more infectious Delta variant (B.1.617.2) is now surging, further deepening the health crises caused by the pandemic. The sharp rise in cases attributed to the Delta variant has made it especially disturbing and is a variant of concern. Fortunately, current vaccines offer protection against known variants of concern, including the Delta variant. However, the Delta variant has exhibited some ability to dodge the immune system as it is found that neutralizing antibodies from prior infections or vaccines are less receptive to binding with the Delta spike protein. Here, we investigated the structural changes caused by the mutations in the Delta variant’s receptor-binding interface and explored the effects on binding with the ACE2 receptor as well as with neutralizing antibodies. We find that the receptor-binding β-loop-β motif adopts an altered but stable conformation causing separation in some of the antibody binding epitopes. Our study shows reduced binding of neutralizing antibodies and provides a possible mechanism for the immune evasion exhibited by the Delta variant.
Keywords: Antibody binding; Delta variant B.1.617.2; Immune escape; Molecular dynamics; SARS-CoV-2 variants.
【저자키워드】 molecular dynamics, Antibody binding, Immune escape, SARS-CoV-2 variants, Delta variant B.1.617.2, 【초록키워드】 neutralizing antibody, Vaccine, pandemic, Mutation, Neutralizing antibodies, B.1.351, variant, Infection, variants of concern, Delta, B.1.617.2, ACE2 receptor, molecular dynamics, immune system, delta variant, variants, immune, Spike protein, immune evasion, Epitopes, Antibody binding, Health, Immune escape, SARS-CoV-2 variants, B.1.1.7, Alpha, Beta, change, mechanism, binding, in some, motif, offer, Effect, initial, caused, investigated, reduced, exhibited, provide, less, 【제목키워드】 implication, changes in, the SARS-CoV-2,