Structural, biochemical and electrostatic basis of serotype specificity in bovine enteroviruses

2.50
Hdl Handle:
http://hdl.handle.net/2436/15444
Title:
Structural, biochemical and electrostatic basis of serotype specificity in bovine enteroviruses
Authors:
Smyth, M.S.; Martin, Jan H.
Abstract:
We have performed immunostructural analyses of three closely related picornaviruses in order to gain understanding of the biochemical and structural basis of serotype specificity. We carried out sequence alignments of the capsid regions of three bovine enterovirus strains: VG-5-27 and M-4 from serotype 1 and PS-87 from serotype 2. Using our knowledge of the three dimensional and antigenic structure of strain VG-5-27 and the high levels of sequence identity between the strains, we have calculated the structures and solvent-accessible electrostatic potentials of the epitopes of all three viruses. We have demonstrated the viability of the molecular models of the epitopes of the M-4 and PS-87 strains. In each of the strains, we have explained the serotype specificities in terms of specific physical and chemical properties, and identified individual residues which are pivotal in determination of antibody recognition. These changes are in agreement with the known cross-reactivity of peptide and antiviral sera, showing that it is possible to derive structures for short variable sections of proteins of high sequence identity using molecular modelling which are significant in terms of biological function. We believe this study to be a novel approach in the analysis of virus serotype specificity.
Citation:
Archives of Virology, 146(2): 347-355
Publisher:
Springer Wien
Issue Date:
2001
URI:
http://hdl.handle.net/2436/15444
DOI:
10.1007/s007050170179
Additional Links:
http://www.springerlink.com/content/2c9a2pr4m7wmpfpf/
Type:
Article
Language:
en
Description:
Metadata only.
ISSN:
03048608,14328798
Appears in Collections:
Cancer Research Group

Full metadata record

DC FieldValue Language
dc.contributor.authorSmyth, M.S.-
dc.contributor.authorMartin, Jan H.-
dc.date.accessioned2007-12-20T12:40:53Z-
dc.date.available2007-12-20T12:40:53Z-
dc.date.issued2001-
dc.identifier.citationArchives of Virology, 146(2): 347-355en
dc.identifier.issn03048608,14328798-
dc.identifier.doi10.1007/s007050170179-
dc.identifier.urihttp://hdl.handle.net/2436/15444-
dc.descriptionMetadata only.en
dc.description.abstractWe have performed immunostructural analyses of three closely related picornaviruses in order to gain understanding of the biochemical and structural basis of serotype specificity. We carried out sequence alignments of the capsid regions of three bovine enterovirus strains: VG-5-27 and M-4 from serotype 1 and PS-87 from serotype 2. Using our knowledge of the three dimensional and antigenic structure of strain VG-5-27 and the high levels of sequence identity between the strains, we have calculated the structures and solvent-accessible electrostatic potentials of the epitopes of all three viruses. We have demonstrated the viability of the molecular models of the epitopes of the M-4 and PS-87 strains. In each of the strains, we have explained the serotype specificities in terms of specific physical and chemical properties, and identified individual residues which are pivotal in determination of antibody recognition. These changes are in agreement with the known cross-reactivity of peptide and antiviral sera, showing that it is possible to derive structures for short variable sections of proteins of high sequence identity using molecular modelling which are significant in terms of biological function. We believe this study to be a novel approach in the analysis of virus serotype specificity.en
dc.language.isoenen
dc.publisherSpringer Wienen
dc.relation.urlhttp://www.springerlink.com/content/2c9a2pr4m7wmpfpf/en
dc.subjectSerotype specificityen
dc.subjectBovine enterovirusesen
dc.subjectPicornavirusesen
dc.subjectVG-5-27en
dc.subjectAnimal viruses-
dc.titleStructural, biochemical and electrostatic basis of serotype specificity in bovine enterovirusesen
dc.typeArticleen
All Items in WIRE are protected by copyright, with all rights reserved, unless otherwise indicated.