Bovine viral diarrhea virus glycoprotein E2 (E2)

Bovine viral diarrhea virus glycoprotein E2 (BVDV E2) is an envelope protein essential for pestivirus entry into host cells, forming disulfide-linked homodimers and heterodimers with E1 that mediate receptor binding and membrane fusion.[1][4] Its ectodomain features a unique three-domain architecture: two Ig-like domains (I and II) followed by an elongated β-stranded domain III with a novel fold, including a conserved histidine (His762) for pH sensing during endosomal acidification and extensive glycosylation and disulfide bonds for stability.[1] E2 determines cellular tropism via interactions with receptors like CD46 and harbors major neutralizing antibody epitopes, particularly in domains I and II.[1][4] Structurally, it lacks classic fusion motifs, suggesting E1 as the primary fusogen with E2 providing scaffold support, a model relevant to related hepatitis C virus.[1] BVDV particles, enriched in cholesterol and sphingolipids, display low E2 abundance on their ~50 nm envelope, highlighting E2's role in morphogenesis and entry.[2][4] As a veterinary pathogen target, E2 inhibition could block bovine infections, though no approved drugs exist.[3][4]

Other names

BVDV E2pestivirus E2