The SD1 Subdomain of Venezuelan Equine Encephalitis Virus Capsid Protein Plays a Critical Role in Nucleocapsid and Particle Assembly


Reynaud, JM; Lulla, V; Kim, DY; Frolova, EI; Frolov, I; (2015) The SD1 Subdomain of Venezuelan Equine Encephalitis Virus Capsid Protein Plays a Critical Role in Nucleocapsid and Particle Assembly. Journal of virology, 90 (4). pp. 2008-2020. ISSN 0022-538X DOI: https://doi.org/10.1128/JVI.02680-15

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Abstract

Venezuelan equine encephalitis virus (VEEV) is an important human and animal pathogen, for which no safe and efficient vaccines or therapeutic means have been developed. Viral particle assembly and budding processes represent potential targets for therapeutic intervention. However, our understanding of the mechanistic process of VEEV assembly, RNA encapsidation, and the roles of different capsid-specific domains in these events remain to be described. The results of this new study demonstrate that the very amino-terminal VEEV capsid-specific subdomain SD1 is a critical player in the particle assembly process. It functions in a virus-specific mode, and its deletion, mutation, or replacement by the same subdomain derived from other alphaviruses has strong negative effects on infectious virus release. VEEV variants with mutated SD1 accumulate adaptive mutations in both SD1 and SD2, which result in a more efficiently replicating phenotype. Moreover, efficient nucleocapsid and particle assembly proceeds only when the two subdomains, SD1 and SD2, are derived from the same alphavirus. These two subdomains together appear to form the central core of VEEV nucleocapsids, and their interaction is one of the driving forces of virion assembly and budding. The similar domain structures of alphavirus capsid proteins suggest that this new knowledge can be applied to other alphaviruses.

Item Type: Article
Keywords: SEMLIKI-FOREST-VIRUS, RNA ENCAPSIDATION, VIRAL GENOME, COILED-COIL, CDNA-CLONE, TRANSCRIPTION, ALPHAVIRUSES, REPLICATION, EVOLUTION, DOMAIN
Faculty and Department: Faculty of Infectious and Tropical Diseases > Dept of Pathogen Molecular Biology
PubMed ID: 26656680
Web of Science ID: 369152700027
URI: http://researchonline.lshtm.ac.uk/id/eprint/2534201

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