| pubmed-article:8406867 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8406867 | lifeskim:mentions | umls-concept:C0038409 | lld:lifeskim |
| pubmed-article:8406867 | lifeskim:mentions | umls-concept:C0003250 | lld:lifeskim |
| pubmed-article:8406867 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:8406867 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:8406867 | lifeskim:mentions | umls-concept:C1152118 | lld:lifeskim |
| pubmed-article:8406867 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:8406867 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:8406867 | pubmed:dateCreated | 1993-11-24 | lld:pubmed |
| pubmed-article:8406867 | pubmed:abstractText | Preliminary analysis indicated that a 19-amino-acid peptide sequence (435 to 453 of GtfC) within a highly conserved region of the glucosyltransferases of the cariogenic streptococci might be functionally important (J.-S. Chia, S.-W. Lin, T.-Y. Hsu, J.-Y. Chen, H.-W. Kwan, and C.-S. Yang, Infect. Immun. 61:1563-1566, 1993). To obtain antipeptide monoclonal antibodies (MAbs), the 19-amino-acid peptide was conjugated to bovine serum albumin and used as an antigen in BALB/c mice. Six immunoglobulin G-secreting hybridoma clones, CJSm18-S1 to -S6, specifically reacted with this peptide and with purified GtfC and GtfD but not with bovine serum albumin in an enzyme-linked immunosorbent assay. The concentrated hybridoma supernatant of all six MAbs inhibited GtfC enzymatic activity but failed to inhibit GtfD, although GtfD contains the same peptide sequence. Further analysis of a purified immunoglobulin G2b MAb from one of the clones, CJSm18-S3, confirmed that this MAb specifically inhibited GtfC enzymatic activity for insoluble-glucan synthesis in a dose-dependent manner. CJSm18-S3, even at high concentrations, had no effect on GtfD, which synthesizes water-soluble glucan exclusively. Furthermore, the in vitro sucrose-dependent adherence of Streptococcus mutans was also inhibited by CJSm18-S3 in a dose-dependent manner. Our results indicate that the peptide containing the N-terminal conserved region of glucosyltransferases is functionally important for both enzymatic activity and bacterial adherence. | lld:pubmed |
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| pubmed-article:8406867 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8406867 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8406867 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8406867 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:8406867 | pubmed:issn | 0019-9567 | lld:pubmed |
| pubmed-article:8406867 | pubmed:author | pubmed-author:ChenJ YJY | lld:pubmed |
| pubmed-article:8406867 | pubmed:author | pubmed-author:YangC SCS | lld:pubmed |
| pubmed-article:8406867 | pubmed:author | pubmed-author:LinS WSW | lld:pubmed |
| pubmed-article:8406867 | pubmed:author | pubmed-author:LinR HRH | lld:pubmed |
| pubmed-article:8406867 | pubmed:author | pubmed-author:ChiaJ SJS | lld:pubmed |
| pubmed-article:8406867 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8406867 | pubmed:volume | 61 | lld:pubmed |
| pubmed-article:8406867 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8406867 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8406867 | pubmed:pagination | 4689-95 | lld:pubmed |
| pubmed-article:8406867 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8406867 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8406867 | pubmed:articleTitle | Inhibition of glucosyltransferase activities of Streptococcus mutans by a monoclonal antibody to a subsequence peptide. | lld:pubmed |
| pubmed-article:8406867 | pubmed:affiliation | Graduate Institute of Microbiology, College of Medicine, National Taiwan University, Taipei, Republic of China. | lld:pubmed |
| pubmed-article:8406867 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8406867 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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