The Nipah virus (NiV)  and Hendra virus (HeV) are highly pathogenic RNA viruses in the genus <i>Henipavirus</i> and the subfamily <i>Paramyxoviridae</i>. Viral replication relies on the interaction between the C-terminal domain, Ntail, of the viral nucleoprotein (N) and the C-terminal X domain, XD, of the viral polymerase co-factor phosphoprotein (P). We are particularly interested in Ntail-XD interactions in either virus, which could be a novel drug target. The Ntail-XD interaction is dynamic in nature and involves a disorder-to-order transition in a specific region of the otherwise disordered Ntail. We examine this interaction using isothermal titration calorimetry (ITC) and site-specific infrared spectroscopy. Single-cysteine mutations to HeV Ntail were introduced at 6 sites and to NiV were introduced at 9 sites, and the cysteine-variant proteins were chemically modified at cysteine to introduce the thiocyano (SCN) group as an infrared probe of the Ntail-XD interactions. Although difficulty with reaching desired concentrations of the cyanylated Ntail proteins has made ITC experiments challenging, the IR spectra provide new pictures of “fuzzy” and quite dynamic bound complexes.

Investigating dynamic protein-protein binding interactions in the Nipah and Hendra virus ntail-XD complexes using the cyanylated cysteine vibrational probe

251st National Meeting (2016)

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