Bovine Corona Virus E2 protein Mouse Monoclonal Antibody [Clone ID: 5A4]

Bovine Corona Virus Spike glycoprotein is cleaved into S1 and S2 Spike proteins. The precursor is processed into S1 and S2 by host cell furin or furin-like protease to yield the mature S1 and S2 proteins. The cleavage site between S1 and S2 requires the optimal sequence KR-X-KR-R.

S1 attaches the virion to the cell membrane by binding to 9-O-acetylated sialic acid containing proteins, initiating the infection.

S2 is a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes.