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Mapping of domains responsible for nucleocapsid protein–phosphoprotein interaction of henipaviruses

¹ Institute of Biological Sciences (Genetics), University of Malaya, 50603 Kuala Lumpur, Malaysia
² Department of Medical Microbiology, University of Malaya, 50603 Kuala Lumpur, Malaysia
³ CSIRO Livestock Industries, Australian Animal Health Laboratory, PO Bag 24, Geelong, Victoria 3220, Australia

Correspondence
L.-F. Wang
Linfa.Wang{at}csiro.au

Hendra virus (HeV) and Nipah virus (NiV) are members of a new genus, Henipavirus, in the family Paramyxoviridae. Each virus encodes a phosphoprotein (P) that is significantly larger than its counterparts in other known paramyxoviruses. The interaction of this unusually large P with its nucleocapsid protein (N) was investigated in this study by using recombinant full-length and truncated proteins expressed in bacteria and a modified protein-blotting protein-overlay assay. Results from our group demonstrated that the N and P of both viruses were able to form not only homologous, but also heterologous, N–P complexes, i.e. HeV N was able to interact with NiV P and vice versa. Deletion analysis of the N and P revealed that there were at least two independent N-binding sites on P and they resided at the N and C termini, respectively. Similarly, more than one P-binding site was present on N and one of these was mapped to a 29 amino acid (aa) C-terminal region, which on its own was sufficient to interact with the extreme C-terminal 165 aa region of P.

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