pubmed-article:2409073 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2409073 | lifeskim:mentions | umls-concept:C0031921 | lld:lifeskim |
pubmed-article:2409073 | lifeskim:mentions | umls-concept:C0018494 | lld:lifeskim |
pubmed-article:2409073 | lifeskim:mentions | umls-concept:C0003316 | lld:lifeskim |
pubmed-article:2409073 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
pubmed-article:2409073 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:2409073 | pubmed:dateCreated | 1985-8-22 | lld:pubmed |
pubmed-article:2409073 | pubmed:abstractText | F-like conjugative pili are expressed by plasmids with closely related transfer systems. They are tubular filaments that are composed of repeating pilin subunits arranged in a helical array. Both F and ColB2 pilin have nearly identical protein sequences, and both contain an acetylated amino-terminal alanine residue. However, they differ by a few amino acid residues at their amino termini. Rabbit antisera raised against purified F and ColB2 pili are immunologically cross-reactive by only 25%, as measured by a competition enzyme-linked immunosorbent assay (ELISA). A tryptic peptide corresponding to the first 15 amino acid residues of ColB2 pilin was isolated and found to remove nearly 80% of ColB2 pilus-directed rabbit antibodies. The corresponding tryptic peptide from F pilin, which reacted with anti-F pilus antibodies to remove 80%, was less than 20% reactive with anti-ColB2 pilus antiserum. Cleavage of these peptides with cyanogen bromide (at a methionine residue approximately in the middle of the peptide) did not affect the antigenicity of these peptides. Synthetic N alpha-acetylated peptides corresponding to the first eight amino acids of F pilin (Ac-Ala-Gly-Ser-Ser-Gly-Gln-Asp-Leu-COOH) and the first six amino acids of ColB2 pilin (Ac-Ala-Gln-Gly-Gln-Asp-Leu-COOH) were prepared and tested by competition ELISA with homologous and heterologous anti-pilus antisera. The F peptide F(1-8) inhibited the interaction of F pili and anti-F pilus antiserum to 80%, while the ColB2 peptide ColB2(1-6) inhibited anti-ColB2 pilus antiserum reacting with ColB2 pili by greater than 60%. The two peptides F(1-8) and ColB2(1-6) were inactive by competition ELISAs with heterologous antisera. These results suggest that the major antigenic determinant of both F and ColB2 pili is at the amino terminus of the pilin subunit and that 80% of antibodies raised against these pili are specific for this region of the pilin molecule. | lld:pubmed |
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pubmed-article:2409073 | pubmed:language | eng | lld:pubmed |
pubmed-article:2409073 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2409073 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:2409073 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2409073 | pubmed:month | Jul | lld:pubmed |
pubmed-article:2409073 | pubmed:issn | 0021-9193 | lld:pubmed |
pubmed-article:2409073 | pubmed:author | pubmed-author:ParkerJ MJM | lld:pubmed |
pubmed-article:2409073 | pubmed:author | pubmed-author:HodgesR SRS | lld:pubmed |
pubmed-article:2409073 | pubmed:author | pubmed-author:ParanchychWW | lld:pubmed |
pubmed-article:2409073 | pubmed:author | pubmed-author:FrostL SLS | lld:pubmed |
pubmed-article:2409073 | pubmed:author | pubmed-author:FinlayB BBB | lld:pubmed |
pubmed-article:2409073 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2409073 | pubmed:volume | 163 | lld:pubmed |
pubmed-article:2409073 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2409073 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2409073 | pubmed:pagination | 331-5 | lld:pubmed |
pubmed-article:2409073 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:2409073 | pubmed:year | 1985 | lld:pubmed |
pubmed-article:2409073 | pubmed:articleTitle | Major antigenic determinants of F and ColB2 pili. | lld:pubmed |
pubmed-article:2409073 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2409073 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:2409073 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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