pubmed-article:2414905 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2414905 | lifeskim:mentions | umls-concept:C0042776 | lld:lifeskim |
pubmed-article:2414905 | lifeskim:mentions | umls-concept:C0014078 | lld:lifeskim |
pubmed-article:2414905 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
pubmed-article:2414905 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
pubmed-article:2414905 | lifeskim:mentions | umls-concept:C0003316 | lld:lifeskim |
pubmed-article:2414905 | lifeskim:mentions | umls-concept:C1446680 | lld:lifeskim |
pubmed-article:2414905 | lifeskim:mentions | umls-concept:C0439064 | lld:lifeskim |
pubmed-article:2414905 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
pubmed-article:2414905 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:2414905 | pubmed:dateCreated | 1985-12-11 | lld:pubmed |
pubmed-article:2414905 | pubmed:abstractText | The neutralization (N) site on the gp56 (E2) surface glycoprotein of the TC-83 vaccine strain of Venezuelan equine encephalomyelitis (VEE) virus has been characterized using monoclonal antibodies. Five new epitopes (E2d-h) were identified three of which could be mapped into the critical N site by using a competitive binding assay (CBA). Antibodies reactive with these three epitopes had either N or N and hemagglutination-inhibition activity. All epitopes contained within this N site elicited monoclonal antibodies that could protect mice from peripheral virus challenge. Antibodies reactive with the N site on other subtypes of VEE virus (IC and II) bound to, but failed to neutralize, TC-83 virus. Epitopes defined by these antibodies could be located outside of the N site on TC-83 virus by CBA. Antigenic activity of all epitopes except E2d was resistant to treatment with 2% SDS, 3% beta-mercaptoethanol, or cleavage with Staphylococcus aureus V8 protease. Those antibodies which defined epitopes located within the N site of TC-83 with CBA bound the same V8 fragments in immunoblots. Those antibodies which defined epitopes not located within the N site bound a different set of fragments than neutralizing antibodies. These results indicate that there is a specific N site on the E2 of VEE virus which undergoes significant antigenic drift while maintaining structural and functional integrity. | lld:pubmed |
pubmed-article:2414905 | pubmed:language | eng | lld:pubmed |
pubmed-article:2414905 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2414905 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2414905 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2414905 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:2414905 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2414905 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2414905 | pubmed:month | Apr | lld:pubmed |
pubmed-article:2414905 | pubmed:issn | 0042-6822 | lld:pubmed |
pubmed-article:2414905 | pubmed:author | pubmed-author:RoehrigJ TJT | lld:pubmed |
pubmed-article:2414905 | pubmed:author | pubmed-author:MathewsJ HJH | lld:pubmed |
pubmed-article:2414905 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2414905 | pubmed:day | 30 | lld:pubmed |
pubmed-article:2414905 | pubmed:volume | 142 | lld:pubmed |
pubmed-article:2414905 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2414905 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2414905 | pubmed:pagination | 347-56 | lld:pubmed |
pubmed-article:2414905 | pubmed:dateRevised | 2005-11-17 | lld:pubmed |
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pubmed-article:2414905 | pubmed:year | 1985 | lld:pubmed |
pubmed-article:2414905 | pubmed:articleTitle | The neutralization site on the E2 glycoprotein of Venezuelan equine encephalomyelitis (TC-83) virus is composed of multiple conformationally stable epitopes. | lld:pubmed |
pubmed-article:2414905 | pubmed:publicationType | Journal Article | lld:pubmed |
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