Structural highlights
Function[NCAP_NIPAV] Encapsidates the genome protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (By similarity). [PHOSP_NIPAV] Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template (By similarity). May play a role to prevent the establishment of cellular antiviral state by binding to host STAT1 in the cytoplasm. This activity is not as strong as that of V and W. Publication Abstract from PubMedNipah virus (NiV) is a highly pathogenic emergent paramyxovirus causing deadly encephalitis in humans. Its replication requires a constant supply of unassembled nucleoprotein (N0) in complex with its viral chaperone, the phosphoprotein (P). To elucidate the chaperone function of P, we reconstituted NiV the N0-P core complex and determined its crystal structure. The binding of the N-terminal region of P blocks the polymerization of N by interfering with subdomain exchange between N protomers and keeps N0 in an open conformation, ready to grasp an RNA molecule. We found that a peptide derived from the N-binding region of P protects cells against viral infection and demonstrated by structure-based mutagenesis that this peptide acts by inhibiting N0-P formation. These results provide new insights about the assembly of N along genomic RNA and validate the N0-P complex as a target for drug development. Structure of Nipah virus unassembled nucleoprotein in complex with its viral chaperone.,Yabukarski F, Lawrence P, Tarbouriech N, Bourhis JM, Delaforge E, Jensen MR, Ruigrok RW, Blackledge M, Volchkov V, Jamin M Nat Struct Mol Biol. 2014 Aug 10. doi: 10.1038/nsmb.2868. PMID:25108352[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 11:43, 25 December 2014.