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A single amino acid substitution in the V protein of Nipah virus alters its ability to block interferon signalling in cells from different species

Nicola Stock^1,

¹ Centre for Biomolecular Sciences, University of St Andrews, The North Haugh, St Andrews KY16 9ST, UK
² Division of Basic Medical Sciences, St George's, University of London, London SW17 0RE, UK
³ CSIRO Livestock Industries, Australian Animal Health Laboratory, Geelong, VIC 3220, Australia

Correspondence
Richard Randall
rer{at}st-andrews.ac.uk

The V protein of the paramyxovirus Nipah virus (NiV) has been shown to antagonize the interferon (IFN) response in human cells via sequestration of STAT1 and STAT2. This study describes a mutant of the NiV V protein, referred to as V(AAHL), that is unable to antagonize IFN signalling and demonstrates that a single amino acid substitution is responsible for its inactivity. The molecular basis for this was identified as a failure to interact with STAT1 and STAT2. It was also shown that NiV V, but not V(AAHL), was functional as an IFN antagonist in human, monkey, rabbit, dog, horse, pig and bat cells, which suggests that the ability of NiV to block IFN signalling is not a major constraint that prevents this virus from crossing species barriers.

Present address: Howard Hughes Medical Institute, Northwestern University, Evanston, IL 60208-3500, USA.

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