Penicillin-binding proteins in Streptococcus mitis
The penicillin-binding protein (PBP) profiles of penicillin-susceptible and -resistant clinical isolates of Streptococcus mitis varied even with strains with similar minimal inhibitory concentrations (MICs). S. mitis NCTC 10712 was used as a DNA recipient to investigate PBP alterations which could o...
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Veröffentlicht in: | Current microbiology 1992-05, Vol.24 (5), p.289-294 |
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Sprache: | eng |
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Zusammenfassung: | The penicillin-binding protein (PBP) profiles of penicillin-susceptible and -resistant clinical isolates of Streptococcus mitis varied even with strains with similar minimal inhibitory concentrations (MICs). S. mitis NCTC 10712 was used as a DNA recipient to investigate PBP alterations which could occur as a result of spontaneous mutation and intra- and interspecific transfer of penicillin resistance genes. S. mitis NCTC 10712 possesses seven major PBPs ranging in molecular mass from 49-82 kDa. Transformants with MICs greater than 1 mu g/ml were obtained with both S. mitis and S. pneumoniae donor DNA. Depending on the source of the donor DNA and level of resistance achieved, transformants showed reduced penicillin-binding affinities of PBPs 2, 3, 4, 5, and 6. The most consistent PBP alteration associated with increasing resistance in S. mitis NCTC 10712 was seen with PBP 3 (74 kDa). |
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ISSN: | 0343-8651 1432-0991 |
DOI: | 10.1007/BF01577335 |