pubmed-article:7785985 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7785985 | lifeskim:mentions | umls-concept:C0038410 | lld:lifeskim |
pubmed-article:7785985 | lifeskim:mentions | umls-concept:C0080194 | lld:lifeskim |
pubmed-article:7785985 | lifeskim:mentions | umls-concept:C1515926 | lld:lifeskim |
pubmed-article:7785985 | lifeskim:mentions | umls-concept:C0525278 | lld:lifeskim |
pubmed-article:7785985 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:7785985 | pubmed:dateCreated | 1995-7-20 | lld:pubmed |
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pubmed-article:7785985 | pubmed:abstractText | The 1.5-kb transpeptidase-encoding region (TER) of penicillin-binding protein (PBP) 2B was amplified and sequenced from 18 penicillin-resistant isolates of Streptococcus pneumoniae, with each isolate representing a different DNA fingerprint profile of the TER. PBP 2B TERs from penicillin-resistant isolates revealed extensive sequence divergence from the penicillin-susceptible R6 strain, differing by up to 170 nucleotide substitutions and resulting in up to 38 alterations in the amino acid sequence of the protein. All penicillin-resistant isolates showed sequence divergence within a +/- 300-bp area at the center of the PBP 2B TER. Although a number of amino acid substitutions were found within this central area of PBP 2B, only two substitutions were common to all resistant isolates, namely, Thr-252 replacement by Ala and Glu-282 replacement by Gly. These two substitutions appear to be essentially associated with a decreased affinity of PBP 2B for penicillin. A second block of divergent nucleotide sequence was prominent amongst isolates with high levels of resistance. This was a +/- 100-bp area of the TER around nucleotide 1300 and included the substitution of Gly for Asp-431, which was the only amino acid substitution within this area that was common to all isolates. These data may assist in the definition of the structural changes in the penicillin-binding site of PBP 2B associated with penicillin resistance in S. pneumoniae. | lld:pubmed |
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pubmed-article:7785985 | pubmed:language | eng | lld:pubmed |
pubmed-article:7785985 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7785985 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:7785985 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7785985 | pubmed:month | Apr | lld:pubmed |
pubmed-article:7785985 | pubmed:issn | 0066-4804 | lld:pubmed |
pubmed-article:7785985 | pubmed:author | pubmed-author:SmithA MAM | lld:pubmed |
pubmed-article:7785985 | pubmed:author | pubmed-author:KlugmanK PKP | lld:pubmed |
pubmed-article:7785985 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7785985 | pubmed:volume | 39 | lld:pubmed |
pubmed-article:7785985 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7785985 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7785985 | pubmed:pagination | 859-67 | lld:pubmed |
pubmed-article:7785985 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:7785985 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:7785985 | pubmed:articleTitle | Alterations in penicillin-binding protein 2B from penicillin-resistant wild-type strains of Streptococcus pneumoniae. | lld:pubmed |
pubmed-article:7785985 | pubmed:affiliation | Department of Medical Microbiology, School of Pathology, South African Institute for Medical Research, Johannesburg. | lld:pubmed |
pubmed-article:7785985 | pubmed:publicationType | Journal Article | lld:pubmed |
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