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The crystal structure of Hazara virus nucleoprotein
Structural highlights
FunctionNCAP_HAZVJ Binds dsRNA and ssRNA and probably participates in the packaging of viral genome (By similarity). In the dsRNA binding mode, the nucleocapsid protein specifically binds to the vRNA panhandle secondary structure formed at the termini of viral genome (By similarity). Does not discriminate between viral and nonviral RNAs through ssRNA binding mode (By similarity). Displays dsDNA endonuclease activity that is sequence non-specific (By similarity).[UniProtKB:P89522] Publication Abstract from PubMedThe nairoviruses include assorted tick-borne bunyaviruses that are emerging as causative infectious diseases among humans and animals. As negative-sense single-stranded RNA (-ssRNA) viruses, nairoviruses encode nucleoprotein (NP) that encapsidates the genomic RNA and further forms ribonucleoprotein complex (RNP) with viral RNA-dependent RNA polymerase (RdRp). We previously revealed that the monomeric NP encoded by Crimean-Congo hemorrhagic fever virus (CCHFV) presents a racket-shaped structure and shows unusual DNA-specific endonuclease activity. To examine the structural and biological variation of nairovirus-encoded NPs, here we systematically solved the crystal structures of NPs encoded by various nairoviruses, including Hazara virus (HAZV), Kupe virus (KUPV), and Erve virus (ERVEV). Combined with biochemical analysis, our results generate a clearer picture to aid in the understanding of the functional diversity of nairovirus-encoded NPs and the formation of nairovirus RNPs. IMPORTANCE: Nairoviruses are consisted of several tick-borne bunyaviruses that are emerging as causative infectious diseases among humans and animals, however, little is known of the nairovirus genome assembling and transcription mechanism. Based on the previous study of CCHFV NP reported by different research groups, here we systematically investigate the structural and functional diversity among three different Nairoviruses, these work provide important information on nairovirus nucleoprotein function and the formation of RNPs. Structural and functional diversity of nairovirus-encoded nucleoproteins.,Wang W, Liu X, Wang X, Dong H, Ma C, Wang J, Liu B, Mao Y, Wang Y, Li T, Yang C, Guo Y J Virol. 2015 Aug 5. pii: JVI.01680-15. PMID:26246561[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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