pubmed-article:2479714 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2479714 | lifeskim:mentions | umls-concept:C0949945 | lld:lifeskim |
pubmed-article:2479714 | lifeskim:mentions | umls-concept:C0205473 | lld:lifeskim |
pubmed-article:2479714 | lifeskim:mentions | umls-concept:C0599934 | lld:lifeskim |
pubmed-article:2479714 | pubmed:dateCreated | 1990-1-3 | lld:pubmed |
pubmed-article:2479714 | pubmed:abstractText | Antibodies to a synthetic peptide corresponding to the 141 to 160 amino acid sequence of the protein VP1 of type O foot-and-mouth disease virus (FMDV) neutralize a wider range of type O isolates than anti-virion serum. Extending this peptide at the amino terminus reduced the number of strains neutralized by the antipeptide sera. Reactions with antisera to peptides representing non-contiguous native sequences showed that it was also possible to increase the number of strains effectively neutralized. Selected substitutions of a single amino acid at position 148 markedly altered the neutralizing specificity of antibodies elicited by the 141 to 160 peptide. In particular, a peptide with an L----S substitution at this position induced antibodies which neutralized a type O and a type A virus equally, and guinea-pigs inoculated with it were protected from challenge with either virus. Attempts to isolate variant viruses resistant to neutralization with anti-peptide antibody indicated that these occurred at low frequency, and there was some evidence that resistance may be partially conferred by mutations outside the peptide sequence. | lld:pubmed |
pubmed-article:2479714 | pubmed:language | eng | lld:pubmed |
pubmed-article:2479714 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2479714 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2479714 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2479714 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2479714 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2479714 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2479714 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2479714 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2479714 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2479714 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2479714 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2479714 | pubmed:month | Nov | lld:pubmed |
pubmed-article:2479714 | pubmed:issn | 0022-1317 | lld:pubmed |
pubmed-article:2479714 | pubmed:author | pubmed-author:FrancisM JMJ | lld:pubmed |
pubmed-article:2479714 | pubmed:author | pubmed-author:BrownFF | lld:pubmed |
pubmed-article:2479714 | pubmed:author | pubmed-author:RowlandsD JDJ | lld:pubmed |
pubmed-article:2479714 | pubmed:author | pubmed-author:FoxJ DJD | lld:pubmed |
pubmed-article:2479714 | pubmed:author | pubmed-author:ParryN RNR | lld:pubmed |
pubmed-article:2479714 | pubmed:author | pubmed-author:ClarkeB EBE | lld:pubmed |
pubmed-article:2479714 | pubmed:author | pubmed-author:BarnettP VPV | lld:pubmed |
pubmed-article:2479714 | pubmed:author | pubmed-author:OuldridgeE... | lld:pubmed |
pubmed-article:2479714 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2479714 | pubmed:volume | 70 ( Pt 11) | lld:pubmed |
pubmed-article:2479714 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2479714 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2479714 | pubmed:pagination | 2919-30 | lld:pubmed |
pubmed-article:2479714 | pubmed:dateRevised | 2003-11-14 | lld:pubmed |
pubmed-article:2479714 | pubmed:meshHeading | pubmed-meshheading:2479714-... | lld:pubmed |
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pubmed-article:2479714 | pubmed:meshHeading | pubmed-meshheading:2479714-... | lld:pubmed |
pubmed-article:2479714 | pubmed:year | 1989 | lld:pubmed |
pubmed-article:2479714 | pubmed:articleTitle | Serological prospects for peptide vaccines against foot-and-mouth disease virus. | lld:pubmed |
pubmed-article:2479714 | pubmed:affiliation | Department of Virology, Wellcome Biotechnology Ltd, Beckenham, Kent, U.K. | lld:pubmed |
pubmed-article:2479714 | pubmed:publicationType | Journal Article | lld:pubmed |
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