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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1995-7-20
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U20067,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U20068,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U20069,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U20070,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U20071,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U20072,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U20073,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U20074,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U20075,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U20076,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U20077,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U20078,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U20079,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U20080,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U20081,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U20082,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U20083,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U20084,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X16022
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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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7785985-1741619,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7785985-1766375,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7785985-1938899,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7785985-2654541,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7785985-2715316,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7785985-271968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7785985-2798106,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7785985-2813426,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7785985-3055171,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7785985-3107125,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7785985-3539010,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7785985-6351730,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7785985-6903436,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7785985-7425601,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7785985-8071243,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7785985-8239609
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0066-4804
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
39
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
859-67
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:7785985-Amino Acid Sequence,
pubmed-meshheading:7785985-Bacterial Proteins,
pubmed-meshheading:7785985-Base Sequence,
pubmed-meshheading:7785985-Carrier Proteins,
pubmed-meshheading:7785985-Hexosyltransferases,
pubmed-meshheading:7785985-Molecular Sequence Data,
pubmed-meshheading:7785985-Multienzyme Complexes,
pubmed-meshheading:7785985-Muramoylpentapeptide Carboxypeptidase,
pubmed-meshheading:7785985-Penicillin Resistance,
pubmed-meshheading:7785985-Penicillin-Binding Proteins,
pubmed-meshheading:7785985-Peptidyl Transferases,
pubmed-meshheading:7785985-Streptococcus pneumoniae
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pubmed:year |
1995
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pubmed:articleTitle |
Alterations in penicillin-binding protein 2B from penicillin-resistant wild-type strains of Streptococcus pneumoniae.
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pubmed:affiliation |
Department of Medical Microbiology, School of Pathology, South African Institute for Medical Research, Johannesburg.
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pubmed:publicationType |
Journal Article
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