| pubmed-article:742510 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:742510 | lifeskim:mentions | umls-concept:C0038409 | lld:lifeskim |
| pubmed-article:742510 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:742510 | lifeskim:mentions | umls-concept:C0439064 | lld:lifeskim |
| pubmed-article:742510 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:742510 | pubmed:dateCreated | 1979-4-25 | lld:pubmed |
| pubmed-article:742510 | pubmed:abstractText | We have isolated a series of five proteins which appear to possess characteristic individual capacities for synthesizing dextrans and binding dextrans. Our suggestion that these proteins comprise an isozyme-like distribution of lectin and enzyme activities is, of course, very speculative and remains to be rigourously confirmed. However, the very identification of these several dextran binding proteins provides a biochemical basis to explain numerous observations suggesting that more than one mechanism for dextran binding is possessed by S. mutans (for instance: 24-27), especially the observations with mutants (24). These proteins probably are the molecular determinants of host infection by S. mutans and may prove to be potent immunogens for use in a vaccine. The presence of a dextran-binding lectin in S. mutans implicates this bacterial lectin in the earliest stage of infection: Attachment to host tissues. The multiplicity of proteins possessing characteristic dextran-synthesizing and dextran-binding capacities indicates the complexity of the adherence mechanisms evolved in S. mutans. Experiments with other bacteria (10-12, 28) suggest that bacterial lectins, in concert with host tissue carbohydrates, may be the molecular mediators of host recognition and subsequent initial attachment of bacterial cells to host tissues in non-pathogenic as well as pathogenic bacteria. | lld:pubmed |
| pubmed-article:742510 | pubmed:language | eng | lld:pubmed |
| pubmed-article:742510 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:742510 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:742510 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:742510 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:742510 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:742510 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:742510 | pubmed:issn | 0065-2598 | lld:pubmed |
| pubmed-article:742510 | pubmed:author | pubmed-author:McCabeM MMM | lld:pubmed |
| pubmed-article:742510 | pubmed:author | pubmed-author:HamelikR MRM | lld:pubmed |
| pubmed-article:742510 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:742510 | pubmed:volume | 107 | lld:pubmed |
| pubmed-article:742510 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:742510 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:742510 | pubmed:pagination | 749-59 | lld:pubmed |
| pubmed-article:742510 | pubmed:dateRevised | 2000-12-18 | lld:pubmed |
| pubmed-article:742510 | pubmed:meshHeading | pubmed-meshheading:742510-D... | lld:pubmed |
| pubmed-article:742510 | pubmed:meshHeading | pubmed-meshheading:742510-B... | lld:pubmed |
| pubmed-article:742510 | pubmed:meshHeading | pubmed-meshheading:742510-C... | lld:pubmed |
| pubmed-article:742510 | pubmed:meshHeading | pubmed-meshheading:742510-C... | lld:pubmed |
| pubmed-article:742510 | pubmed:meshHeading | pubmed-meshheading:742510-S... | lld:pubmed |
| pubmed-article:742510 | pubmed:year | 1978 | lld:pubmed |
| pubmed-article:742510 | pubmed:articleTitle | Multiple forms of dextran-binding proteins from Streptococcus mutans. | lld:pubmed |
| pubmed-article:742510 | pubmed:publicationType | Journal Article | lld:pubmed |
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