Intermolecular interactions in a two-layered viral capsid that requires a complex symmetry mismatch


Limn, CK; Roy, P; (2003) Intermolecular interactions in a two-layered viral capsid that requires a complex symmetry mismatch. Journal of virology, 77 (20). pp. 11114-11124. ISSN 0022-538X DOI: https://doi.org/10.1128/jvi.77.20.11114-11124.2003

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Abstract

The surface of the bluetongue virus core forms a T=13 quasiequivalent icosahedral protein shell with 260 trimers of a single gene product: VP7 protein. Underneath is a smooth layer, made up of VP3 protein, which appears to guide and nucleate the assembly of VP7 trimers. The contacts between the two shells are extensive but nonspecific, and construction of the T=13 icosahedral shell requires polymorphism in the association of the VP7 subunits, each of which has two domains that contribute to trimer formation. We used structural and relative sequence information to guide an investigation of how such a complex structure is achieved during virus assembly and what residues are required to form a stable capsid. Fifteen single or multiple site-specific substitution mutations were introduced into the helical domain of VP7, which is closely associated with the VP3 layer, and the effects on capsid assembly were analyzed. Our data show that both the position and the nature of single residues are critical for the attachment of VP7 to VP3 and that formation of a stable VP7 lattice is not the automatic consequence of trimer formation.

Item Type: Article
Keywords: *Molecular Interaction, *Virus Capsid, Bluetongue Orbivirus, Virus Mutation, Site Directed Mutagenesis, Protein Protein Interaction, Nonhuman, Animal Cell, Article, Priority Journal, *Virus Protein, *Gene Product, *protein vp7, Unclassified Drug, Amino Acid Sequence, Capsid Proteins, chemistry, Molecular Sequence Data, Mutation, Protein Structure, Secondary, Support, Non-U.S. Gov't, Virion, chemistry, Virus Assembly
Faculty and Department: Faculty of Infectious and Tropical Diseases > Dept of Pathogen Molecular Biology
PubMed ID: 14512559
Web of Science ID: 185686100037
URI: http://researchonline.lshtm.ac.uk/id/eprint/15990

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