Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1992-2-14
pubmed:databankReference
pubmed:abstractText
Penicillin resistance in pneumococci is due to the appearance of high molecular-weight penicillin-binding proteins (PBPs) that have reduced affinity for the antibiotic. We have compared the PBX 2x genes (pbpX) of one penicillin-susceptible and five penicillin-resistant clinical isolates of Streptococcus pneumoniae isolated from various parts of the world. All of the resistant isolates contained a low-affinity form of PBP 2x. The 2 kb region of the two penicillin-susceptible isolates differed at only eight nucleotide sites (0.4%) and resulted in one single amino acid difference in PBP 2x. In contrast, the sequences of the PBP 2x genes from the resistant isolates differed overall from those of the susceptible isolates at between 7 and 18% of nucleotide sites and resulted in between 27 and 86 amino acid substitutions in PBP 2x. The altered PBP 2x genes consisted of regions that were similar to those of susceptible strains (less than 3% diverged), alternating with regions that were very different (18-23% diverged). The presence of highly diverged regions within the PBP 2x genes of the resistant isolates contrasts with the uniformity of the sequences of the amylomaltase genes from the same isolates, and with the uniformity of the PBP 2x genes in the two susceptible isolates. It suggests that the altered PBP 2x genes have arisen by localized interspecies recombinational events involving the PBP 2x genes of closely related streptococci, as has been suggested to occur for altered PBP 2b genes (Dowson et al., 1989b). The PBP 2x genes from the resistant isolates could transform the susceptible strain R6 to increased levels of resistance to beta-lactam antibiotics, indicating that the altered forms of PBP 2x in the resistant isolates contribute to their resistance to penicillin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0950-382X
pubmed:author
pubmed:issnType
Print
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1993-2002
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:1766375-Amino Acid Sequence, pubmed-meshheading:1766375-Bacterial Proteins, pubmed-meshheading:1766375-Base Sequence, pubmed-meshheading:1766375-Biological Evolution, pubmed-meshheading:1766375-Carrier Proteins, pubmed-meshheading:1766375-Genetic Variation, pubmed-meshheading:1766375-Glycogen Debranching Enzyme System, pubmed-meshheading:1766375-Hexosyltransferases, pubmed-meshheading:1766375-Humans, pubmed-meshheading:1766375-Molecular Sequence Data, pubmed-meshheading:1766375-Muramoylpentapeptide Carboxypeptidase, pubmed-meshheading:1766375-Penicillin Resistance, pubmed-meshheading:1766375-Penicillin-Binding Proteins, pubmed-meshheading:1766375-Peptidyl Transferases, pubmed-meshheading:1766375-Pneumococcal Infections, pubmed-meshheading:1766375-Recombination, Genetic, pubmed-meshheading:1766375-Sequence Homology, Nucleic Acid, pubmed-meshheading:1766375-Species Specificity, pubmed-meshheading:1766375-Streptococcus pneumoniae, pubmed-meshheading:1766375-Transformation, Bacterial
pubmed:year
1991
pubmed:articleTitle
Interspecies recombinational events during the evolution of altered PBP 2x genes in penicillin-resistant clinical isolates of Streptococcus pneumoniae.
pubmed:affiliation
Max-Planck Institut für Molekelare Genetik, Berlin, Germany.
pubmed:publicationType
Journal Article