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dc.contributor.authorVerdaguer, Núria-
dc.contributor.authorSchoehn, Guy-
dc.contributor.authorOchoa, Wendy F.-
dc.contributor.authorFita, Ignacio-
dc.contributor.authorBrookes, Sharon-
dc.contributor.authorKing, Andrew-
dc.contributor.authorDomingo, Esteban-
dc.contributor.authorMateu, Mauricio G.-
dc.contributor.authorStuart, David I.-
dc.contributor.authorHewat, Elizabeth A.-
dc.identifierdoi: 10.1006/viro.1998.9554-
dc.identifierissn: 0042-6822-
dc.identifier.citationVirology 255(2): 260-268 (1999)-
dc.description.abstractThe interaction of foot-and-mouth disease virus (FM DV) serotype C (clone C-S8c1) with a strongly neutralising monoclona antibody (MAb) 4C4 has been studied by combining data from cryoelectron microscopy and x-ray crystallography. The MAb 404 binds to the exposed flexible GH-loop of viral protein 1 (VP1), which appears to retain its flexibility, allowing movement of the bound Fab. This is in striking contrast to MAb SD6, which binds to the same GH-loop of VP1 but exhibits no movement of the bound lab when observed under identical conditions. However, MAbs 4C4 and SD6 have very similar neutralisation characteristics. The known atomic structure of FM DV C-S8cl and that of the 4C4 Fab cocrystallised with a synthetic peptide corresponding to the GH-loop of VP1 were fitted to the cryoelectron microscope density map. The best fit of the 4C4 Fab is compatible only with monovalent binding of the MAb in agreement with the neutralisation data on 404 MAbs, Fab2s, and labs. The position of the bound GH-loop is related to other known positions of this loop by a hinge rotation about the base of the loop. The 4C4 Fab appears to interact almost exclusively with the G-H loop of VP1, making no other contacts with the viral capsid.-
dc.publisherAcademic Press-
dc.titleFlexibility of the major antigenic loop of foot-and-mouth disease virus bound to a Fab fragment of a neutralising antibody: Structure and neutralisation-
dc.description.versionPeer Reviewed-
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