Dissecting the roles of VP0 cleavage and RNA packaging in picornavirus capsid stabilization: the structure of empty capsids of foot-and-mouth disease virus.

Empty capsids of foot-and-mouth disease virus (FMDV) type A22 Iraq 24/64, whose structure has been solved by X-ray crystallography, are unusual for picornaviruses since they contain VP2 and VP4, the cleavage products of the protein precursor VP0. Both the N terminus of VP1 and the C terminus of VP4,...

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Main Authors: Curry, S, Fry, E, Blakemore, W, Abu-Ghazaleh, R, Jackson, T, King, A, Lea, S, Newman, J, Stuart, D
Formato: Artigo
Idioma:Inglês
Publicado em: 1997
Assuntos:
Research Article
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC230284/
https://ncbi.nlm.nih.gov/pubmed/9371640
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