Molecular basis for occlusion of the jeilongvirus receptor-binding site by the elongated C-terminus.

ABSTRACT: Paramyxoviral transmission between hosts may be, in part, attributed to the ability of the viral envelope-displayed receptor-binding protein (RBP) to bind to cell surface receptors of different host species. We sought to elucidate the architecture of the receptor-binding head region of the RBPs presented by jeilongviruses, a group of emerging and genetically unique paramyxoviruses belonging to the genus Jeilongvirus, family Paramyxoviridae. Structure determination of J and Beilong jeilongvirus RBPs reveals that the proteins exhibit a prototypical six-bladed β-propeller fold, present a binding site with residues associated with sialic acid recognition and hydrolysis, and bear a close structural relationship with sialic acid binding hemagglutinin-neuraminidase (HN)-type paramyx

SUBMITTER: Stelfox AJ 

PROVIDER: S-EPMC12802151 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature