Probing the functions of the paramyxovirus glycoproteins F and HN with a panel of synthetic antibodies.

ABSTRACT: Paramyxoviruses are enveloped negative-strand RNA viruses that are significant human and animal pathogens. Most paramyxoviruses infect host cells via the concerted action of a tetrameric attachment protein (variously called HN, H, or G) that binds either sialic acid or protein receptors on target cells and a trimeric fusion protein (F) that merges the viral envelope with the plasma membrane at neutral pH. F initially folds to a metastable prefusion conformation that becomes activated via a cleavage event during cellular trafficking. Upon receptor binding, the attachment protein, which consists of a globular head anchored to the membrane via a helical tetrameric stalk, triggers a major conformation change in F which results in fusion of virus and host cell membranes. We recently proposed a

SUBMITTER: Welch BD 

PROVIDER: S-EPMC4178754 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature