Synthesis of penicillin-binding proteins in penicillin-treatedStreptococcus pneumoniae

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Identical penicillin-binding domains in penicillin-binding proteins of Streptococcus pneumoniae clinical isolates with different levels of beta-lactam resistance.

We have sequenced the penicillin-binding domains of the complete repertoire of penicillin-binding proteins and MurM from 22 clinical isolates of Streptococcus pneumoniae that span a wide range of beta-lactam resistance levels. Evidence of mosaicism was found in the genes encoding PBP 1a, PBP 2b, PBP 2x, MurM, and, possibly, PBP 2a. Five isolates were found to have identical PBP and MurM sequenc...

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Identical Penicillin-Binding Domains in Penicillin-Binding Proteins of Streptococcus pneumoniae Clinical Isolates with Different Levels of -Lactam Resistance

We have sequenced the penicillin-binding domains of the complete repertoire of penicillin-binding proteins and MurM from 22 clinical isolates of Streptococcus pneumoniae that span a wide range of -lactam resistance levels. Evidence of mosaicism was found in the genes encoding PBP 1a, PBP 2b, PBP 2x, MurM, and, possibly, PBP 2a. Five isolates were found to have identical PBP and MurM sequences, ...

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Interaction of penicillin with the bacterial cell: penicillin-binding proteins and penicillin-sensitive enzymes.

INTRODUCTION ........................................................ 291 General ............... ......................................... 291 Cell Waill Structure and Synthesis ....................... ........................ 292 Identification of the Target of Penicillin Action .......... ........................ 293 PENICILLIN-BINDING COMPONENTS .............. .......................... 296...

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Penicillin-binding proteins in Clostridium perfringens.

The penicillin-binding proteins (PBPs) of Clostridium perfringens were studied. Six PBPs ranging in molecular weight from approximately 42,000 to 100,000 were detected in the cytoplasmic membrane. The relative affinities of the PBPs for 16 beta-lactam antibiotics were determined. Most of the drug saturated PBP 3 and 4 at concentrations equal to their minimal inhibitory concentrations, suggestin...

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Penicillin-binding proteins in Borrelia burgdorferi.

Penicillin-binding proteins were identified in Borrelia burgdorferi membranes. A 94-kilodalton penicillin-binding protein was the first to be labeled with tritiated penicillin and was the first band to disappear in a competition experiment. Its binding ability was destroyed when membranes were preboiled. In addition, several of these penicillin-binding proteins comigrated with bands previously ...

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ژورنال

عنوان ژورنال: FEMS Microbiology Letters

سال: 1984

ISSN: 0378-1097,1574-6968

DOI: 10.1111/j.1574-6968.1984.tb00745.x