Monomeric ephrinB2 binding induces allosteric changes in Nipah virus G that precede its full activation.

ABSTRACT: Nipah virus is an emergent paramyxovirus that causes deadly encephalitis and respiratory infections in humans. Two glycoproteins coordinate the infection of host cells, an attachment protein (G), which binds to cell surface receptors, and a fusion (F) protein, which carries out the process of virus-cell membrane fusion. The G protein binds to ephrin B2/3 receptors, inducing G conformational changes that trigger F protein refolding. Using an optical approach based on second harmonic generation, we show that monomeric and dimeric receptors activate distinct conformational changes in G. The monomeric receptor-induced changes are not detected by conformation-sensitive monoclonal antibodies or through electron microscopy analysis of G:ephrinB2 complexes. However, hydrogen/deuterium exchange exp

SUBMITTER: Wong JJW 

PROVIDER: S-EPMC5626764 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature