Unprocessed foot-and-mouth disease virus capsid precursor displays discontinuous epitopes involved in viral neutralization

Juan-Carlos Saiz, Jordi Cairo, Miguel Medina, Douwe Zuidema, Charles Abrams, Graham Belsham, Esteban Domingo, Just M. Vlak

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

A foot-and-mouth disease virus (FMDV) cDNA cassette containing sequences encoding the capsid precursor P1, peptide 2A and a truncated 2B (abbreviated P1-2A) of type C FMDV, has been modified to generate the authentic amino terminus and the myristoylation signal. This construct has been used to produce a recombinant baculovirus (AcMM53) which. upon infection of Spodoptera frugiperda insect cells, expressed a recombinant P1-2A precursor with a high yield. This polyprotein reacted with neutralizing monoclonal antibodies (MAbs) that bind to continuous epitopes of the major antigenic site A (also termed site 1) of capsid protein VP1. Unexpectedly, it also reacted with neutralizing MAbs which define complex, discontinuous epitopes previously identified on FMDV particles. The reactivity of MAbs with P1-2A was quantitatively similar to their reactivity with intact virus and, in both cases, the reactivity with MAbs that recognized discontinuous epitopes was lost upon heat denaturation of the antigen. The finding that a capsid precursor may fold in such a way as to maintain discontinuous epitopes involved in virus neutralization present on the virion surface opens the possibility of using unprocessed capsid precursors as novel antiviral immunogens.
Original languageEnglish
JournalJournal of Virology
Volume68
Issue number7
Pages (from-to)4557-4564
ISSN0022-538X
Publication statusPublished - 1994
Externally publishedYes

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