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The SARS-CoV-2 spike glycoprotein is a large, trimeric class I fusion protein found on the surface of the virus. It mediates viral entry into host cells by binding to the angiotensin-converting enzyme 2 (ACE2) receptor and facilitating membrane fusion. The Omicron BA.1 variant features numerous mutations in its spike protein, which impact its structure, function, and antigenicity. The Omicron BA.1 variant contains over thirty mutations within its spike protein compared to earlier strains; notable substitutions/deletions include: A67V, H69del, V70del, T95I, G142D, V143del, Y144del, Y145del, N211del, L212I, ins214EPE, G339D, S371L, S373P, S375F, K417N, N440K, G446S, S477N, T478K, E484A, Q493R, G496S, Q498R, N501Y, Y505H, T547K, D614G, H655Y, N679K, P681H, N764K, D796Y, N856K, Q954H, N969K, L981F. These changes alter antigenic properties and enhance transmissibility/immune evasion relative to previous variants such as Delta or Alpha.
Neutralizing antibodies bind to the spike protein, preventing ACE2 binding and/or membrane fusion. Vaccines elicit an antibody response against the spike protein.
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