@article{mbs:/content/journal/jgv/10.1099/vir.0.19752-0, author = "Chan, Y. P. and Koh, C. L. and Lam, S. K. and Wang, L.-F.", title = "Mapping of domains responsible for nucleocapsid protein–phosphoprotein interaction of henipaviruses", journal= "Journal of General Virology", year = "2004", volume = "85", number = "6", pages = "1675-1684", doi = "https://doi.org/10.1099/vir.0.19752-0", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.19752-0", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = " 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.", }