| pubmed-article:12917457 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12917457 | lifeskim:mentions | umls-concept:C0014667 | lld:lifeskim |
| pubmed-article:12917457 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:12917457 | lifeskim:mentions | umls-concept:C0026336 | lld:lifeskim |
| pubmed-article:12917457 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:12917457 | lifeskim:mentions | umls-concept:C0006933 | lld:lifeskim |
| pubmed-article:12917457 | lifeskim:mentions | umls-concept:C0872192 | lld:lifeskim |
| pubmed-article:12917457 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
| pubmed-article:12917457 | pubmed:issue | Pt 9 | lld:pubmed |
| pubmed-article:12917457 | pubmed:dateCreated | 2003-8-14 | lld:pubmed |
| pubmed-article:12917457 | pubmed:abstractText | Mouse monoclonal antibodies (mAbs) were employed to select neutralization escape mutants of equine rhinitis A virus (ERAV). Amino acid changes in the ERAV mutants resulting in resistance to neutralization were identified in capsid protein VP1 at Lys-114, Pro-240 and Thr-241. Although the changes were located in different parts of the polypeptide chain, these mutants exhibited cross-resistance against all four mAbs employed, indicating that these residues contribute to a single immunogenic site. To explain this result, we constructed a model of the three-dimensional structure of the ERAV capsid based on comparison with the closely related foot-and-mouth disease virus (FMDV O(1)). According to this model, VP1 is folded so that Lys-114 is in the beta E-beta F loop of the polypeptide chain at a considerable distance from Pro-240 and Trp-241 in the C-terminal region. However, around the fivefold axis of symmetry, the C terminus of VP1 in each protomer extends to the beta E-beta F loop of the adjacent VP1 in the next protomer. We therefore propose that the immunogenic site in ERAV is formed as a result of the close proximity of the Lys-114 residue in the beta E-beta F loop of one VP1 molecule and of the Pro-240/Thr-241 residues in the adjacent VP1 polypeptide chain. In terms of the overall architecture of the viral capsid structure, this site in ERAV most closely resembles the immunogenic site 1 of FMDV O(1). | lld:pubmed |
| pubmed-article:12917457 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12917457 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12917457 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12917457 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12917457 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12917457 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:12917457 | pubmed:issn | 0022-1317 | lld:pubmed |
| pubmed-article:12917457 | pubmed:author | pubmed-author:ShiehC CCC | lld:pubmed |
| pubmed-article:12917457 | pubmed:author | pubmed-author:KuechlerErnst... | lld:pubmed |
| pubmed-article:12917457 | pubmed:author | pubmed-author:StuartDavidD | lld:pubmed |
| pubmed-article:12917457 | pubmed:author | pubmed-author:LeaSusanS | lld:pubmed |
| pubmed-article:12917457 | pubmed:author | pubmed-author:WutzGordanaG | lld:pubmed |
| pubmed-article:12917457 | pubmed:author | pubmed-author:KriegshäuserG... | lld:pubmed |
| pubmed-article:12917457 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12917457 | pubmed:volume | 84 | lld:pubmed |
| pubmed-article:12917457 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12917457 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12917457 | pubmed:pagination | 2365-73 | lld:pubmed |
| pubmed-article:12917457 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:12917457 | pubmed:meshHeading | pubmed-meshheading:12917457... | lld:pubmed |
| pubmed-article:12917457 | pubmed:meshHeading | pubmed-meshheading:12917457... | lld:pubmed |
| pubmed-article:12917457 | pubmed:meshHeading | pubmed-meshheading:12917457... | lld:pubmed |
| pubmed-article:12917457 | pubmed:meshHeading | pubmed-meshheading:12917457... | lld:pubmed |
| pubmed-article:12917457 | pubmed:meshHeading | pubmed-meshheading:12917457... | lld:pubmed |
| pubmed-article:12917457 | pubmed:meshHeading | pubmed-meshheading:12917457... | lld:pubmed |
| pubmed-article:12917457 | pubmed:meshHeading | pubmed-meshheading:12917457... | lld:pubmed |
| pubmed-article:12917457 | pubmed:meshHeading | pubmed-meshheading:12917457... | lld:pubmed |
| pubmed-article:12917457 | pubmed:meshHeading | pubmed-meshheading:12917457... | lld:pubmed |
| pubmed-article:12917457 | pubmed:meshHeading | pubmed-meshheading:12917457... | lld:pubmed |
| pubmed-article:12917457 | pubmed:meshHeading | pubmed-meshheading:12917457... | lld:pubmed |
| pubmed-article:12917457 | pubmed:meshHeading | pubmed-meshheading:12917457... | lld:pubmed |
| pubmed-article:12917457 | pubmed:meshHeading | pubmed-meshheading:12917457... | lld:pubmed |
| pubmed-article:12917457 | pubmed:meshHeading | pubmed-meshheading:12917457... | lld:pubmed |
| pubmed-article:12917457 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12917457 | pubmed:articleTitle | Model of the equine rhinitis A virus capsid: identification of a major neutralizing immunogenic site. | lld:pubmed |
| pubmed-article:12917457 | pubmed:affiliation | Max F. Perutz Laboratories, University Departments at the Vienna Biocenter, Department of Medical Biochemistry, Division of Biochemistry, University of Vienna, Dr Bohr Gasse 9/3, A-1030 Vienna, Austria. | lld:pubmed |
| pubmed-article:12917457 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12917457 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:12917457 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12917457 | lld:pubmed |
