Bovine coronavirus spike protein (BCoV S protein)

The Bovine coronavirus spike protein is a large trimeric glycoprotein present on the surface of the virus that plays a central role in viral infection by mediating host cell attachment and entry[1][2][4][7][8]. It is subdivided into S1 and S2 subunits; the S1 subunit contains the receptor-binding domain, which recognizes sugars (notably 5-N-acetyl-9-O-acetylneuraminic acid) on host cells, facilitating viral attachment[2][7][8]. The S2 subunit controls membrane fusion, allowing the virus to deliver its RNA genome into the host cell[1][4][5][10]. Structurally, the spike protein has a human galectin-like fold in its N-terminal domain, indicative of evolutionary adaptation from host lectins to accommodate viral receptor specificity[2][7]. The spike protein is a target for the host immune response, and its variability influences the scope of immunity and the effectiveness of diagnostics and therapeutics[8][9]. The spike protein is a major determinant of host range and pathogenicity, and mutations in its receptor-binding domain drive viral evolution and cross-species transmission[8].

Other names

BCoV S proteinSpike glycoproteinS proteinSurface glycoprotein

Inhibition of viral entry (by blocking spike protein-receptor interaction or fusion process); Neutralization by antibodies binding to epitopes in S1 or S2