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

• DOI: 10.1038/s41467-017-00863-3
• Publication Date: 2017-09-27T16:10:42Z
• Authors: Joyce J. W. Wong; Tracy A. Young; Jiayan Zhang; Shiheng Liu; George P. Leser; Elizabeth A. Komives; Robert A. Lamb; Z. Hong Zhou; Joshua Salafsky; Theodore S. Jarde...
• Keywords: Conformational change; Sendai virus

Nipah virus is an emergent paramyxovirus that causes deadly encephalitis and respiratory infections in humans. Two glycoproteins coordinate the infection of host cells, attachment protein (G), which binds to cell surface receptors, a fusion (F) protein, carries out process virus-cell membrane fusion. The G ephrin B2/3 inducing conformational changes trigger F refolding. Using optical approach based on second harmonic generation, we show monomeric dimeric receptors activate distinct G. receptor-induced are not detected by conformation-sensitive monoclonal antibodies or through electron microscopy analysis G:ephrinB2 complexes. However, hydrogen/deuterium exchange experiments confirm generation observations reveal allosteric receptor binding F-activating stalk domains, providing insights into pathway receptor-activated entry.Nipah Here authors use multidisciplinary study viral its ephrinB2 discuss implications for entry.