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The Spike glycoprotein of SARS-CoV‑2 is a large, trimeric class I viral fusion protein that protrudes from the surface of coronavirus particles. It mediates attachment to host cells by specifically binding to the angiotensin-converting enzyme 2 (ACE2) receptor through its receptor-binding domain. The Beta variant (lineage B.1.351) contains key amino acid substitutions—K417N, E484K, N501Y—in its receptor-binding domain that increase infectivity and confer partial resistance to neutralizing antibodies generated against earlier strains. The spike is heavily glycosylated and undergoes proteolytic cleavage at specific sites during maturation and entry processes. As it plays an essential role in viral entry and is highly immunogenic, it serves as both a major therapeutic target for monoclonal antibody drugs and the principal antigen in most COVID‑19 vaccines.[1][2][3][4]
Neutralization of virus by blocking ACE2 binding site on spike RBD[1][3] Inhibition of conformational changes required for membrane fusion – Induction of protective immune responses via vaccination
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