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| | {{STRUCTURE_1fmd| PDB=1fmd | SCENE= }} | | {{STRUCTURE_1fmd| PDB=1fmd | SCENE= }} |
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| - | '''THE STRUCTURE AND ANTIGENICITY OF A TYPE C FOOT-AND-MOUTH DISEASE VIRUS'''
| + | ===THE STRUCTURE AND ANTIGENICITY OF A TYPE C FOOT-AND-MOUTH DISEASE VIRUS=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8081743}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8081743 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8081743}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Icosahedral virus]] | | [[Category: Icosahedral virus]] |
| | [[Category: Virus]] | | [[Category: Virus]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:29:58 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:28:52 2008'' |
Revision as of 00:28, 1 July 2008
Template:STRUCTURE 1fmd
THE STRUCTURE AND ANTIGENICITY OF A TYPE C FOOT-AND-MOUTH DISEASE VIRUS
Template:ABSTRACT PUBMED 8081743
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
Page seeded by OCA on Tue Jul 1 03:28:52 2008
