1fmd
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(New page: 200px<br /><applet load="1fmd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fmd, resolution 3.5Å" /> '''THE STRUCTURE AND ANT...)
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Revision as of 21:54, 24 November 2007
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THE STRUCTURE AND ANTIGENICITY OF A TYPE C FOOT-AND-MOUTH DISEASE VIRUS
Overview
BACKGROUND: Picornaviruses are responsible for a wide range of mammalian, diseases and, in common with other RNA viruses, show considerable, antigenic variation. Foot-and-mouth disease viruses (FMDVs) constitute one, genus of the picornavirus family and are classified into seven serotypes, each of which shows considerable intratypic variation. This antigenic, variation leads to continuing difficulties in controlling the disease. To, date the structure of only one serotype, O, has been reported. RESULTS:, The three-dimensional structure of a serotype C (isolate C-S8c1) FMDV, has, been determined crystallographically at 3.5 A resolution. The main chain, conformation of the virion is very similar to that of type O1 virus. The, immunodominant G-H loop of VP1, the presumed site of cell attachment, is, disordered in both types of virus indicating a functional role for, flexibility of this region. There are significant changes in the structure, of other antigenic loops and in some internal regions involved in, protomer-protomer contacts, including the entire amino-terminal portion of, VP2, described here for the first time for a picornavirus. Antigenic sites, have been identified by genetic and peptide mapping methods, and located, on the capsid. The data reveal a major new discontinuous antigenic site, (site D) which is located near to the three-fold axis and involves, residues of VP1, VP2 and VP3 which lie adjacent to each other on the, capsid. CONCLUSION: In FMDV type C, amino acid substitutions seen in, mutants that are resistant to neutralization by monoclonal antibodies, (MAbs) map to predominantly surface-oriented residues with, solvent-accessible side-chains not involved in interactions with other, amino acids, whereas residues which are accessible but not substituted are, found to be more frequently involved in protein-protein interactions. This, provides a molecular interpretation for the repeated isolation of the same, amino acid substitutions in MAb-resistant variants, an observation, frequently made with RNA viruses. This first comparison of two FMDV, serotypes shows how subtle changes at antigenic sites are sufficient to, cause large changes in antigenic specificity between serotypes.
About this Structure
1FMD is a Protein complex structure of sequences from Foot-and-mouth disease virus. Full crystallographic information is available from OCA.
Reference
The structure and antigenicity of a type C foot-and-mouth disease virus., Lea S, Hernandez J, Blakemore W, Brocchi E, Curry S, Domingo E, Fry E, Abu-Ghazaleh R, King A, Newman J, et al., Structure. 1994 Feb 15;2(2):123-39. PMID:8081743
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