Mutational analysis of Rift Valley fever phlebovirus nucleocapsid protein indicates novel conserved, functional amino acids

Rift Valley fever phlebovirus (RVFV; Phenuiviridae, Phlebovirus) is an important mosquito-borne pathogen of both humans and ruminants. The RVFV genome is composed of tripartite, single stranded, negative or ambisense RNAs. The small (S) segment encodes both the nucleocapsid protein (N) and the non-s...

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Vydáno v:	PLoS neglected tropical diseases Ročník 11; číslo 12; s. e0006155
Hlavní autoři:	Mottram, Timothy J., Li, Ping, Dietrich, Isabelle, Shi, Xiaohong, Brennan, Benjamin, Varjak, Margus, Kohl, Alain
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	United States Public Library of Science 21.12.2017 Public Library of Science (PLoS)
Témata:	Amino Acid Sequence Amino acids Analysis Animals Antiviral agents Aquatic insects Biology and life sciences Capacity Cell Line Coccidioidomycosis Cricetinae DNA Mutational Analysis DNA-directed RNA polymerase Encapsidation Gene mutation Gene sequencing Genetic aspects Genome, Viral - genetics Genomes Health aspects Interactions Life cycle Life cycle engineering Life cycles Medicine and health sciences N protein Nucleic acids Nucleocapsid Proteins - genetics Nucleocapsids Packaging Protein Multimerization - genetics Protein Multimerization - physiology Proteins Research and Analysis Methods Ribonucleic acid Rift Valley fever Rift Valley Fever - virology Rift Valley fever virus - genetics Risk factors RNA RNA, Viral - genetics RNA-Binding Proteins - genetics RNA-directed RNA polymerase Sequence Alignment Transcription Tropical diseases Vector-borne diseases Viral diseases Viral infections Virology Virus Replication Viruses
ISSN:	1935-2735, 1935-2727, 1935-2735
On-line přístup:	Získat plný text
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Popis
Shrnutí:	Rift Valley fever phlebovirus (RVFV; Phenuiviridae, Phlebovirus) is an important mosquito-borne pathogen of both humans and ruminants. The RVFV genome is composed of tripartite, single stranded, negative or ambisense RNAs. The small (S) segment encodes both the nucleocapsid protein (N) and the non-structural protein (NSs). The N protein is responsible for the formation of the viral ribonucleoprotein (RNP) complexes, which are essential in the virus life cycle and for the transcription and replication of the viral genome. There is currently limited knowledge surrounding the roles of the RVFV nucleocapsid protein in viral infection other than its key functions: N protein multimerisation, encapsidation of the RNA genome and interactions with the RNA-dependent RNA polymerase, L. By bioinformatic comparison of the N sequences of fourteen phleboviruses, mutational analysis, minigenome assays and packaging assays, we have further characterised the RVFV N protein. Amino acids P11 and F149 in RVFV N play an essential role in the function of RNPs and are neither associated with N protein multimerisation nor known nucleocapsid protein functions and may have additional roles in the virus life cycle. Amino acid Y30 exhibited increased minigenome activity despite reduced RNA binding capacity. Additionally, we have determined that the N-terminal arm of N protein is not involved in N-L interactions. Elucidating the fundamental processes that involve the nucleocapsid protein will add to our understanding of this important viral protein and may influence future studies in the development of novel antiviral strategies.
Bibliografie:	new_version ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 The authors have declared that no competing interests exist. Current address: Experimental Medicine, Nuffield Department of Medicine, University of Oxford, Oxford, United Kingdom.
ISSN:	1935-2735 1935-2727 1935-2735
DOI:	10.1371/journal.pntd.0006155