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Site-specific mutagenesis analysis of PBP 1A from a penicillin-cephalosporin-resistant pneumococcal isolate.

ABSTRACT: Our mutagenesis study has investigated all amino acid mutations in the penicillin-binding domain of PBP 1A from Hungarian pneumococcal isolate 3191 to determine the importance of every mutation in the development of penicillin and cefotaxime resistance. Our data reveal that mutations at amino acid positions 574 to 577 and position 539 cause penicillin and cefotaxime resistance.

SUBMITTER: Smith AM

PROVIDER: S-EPMC149026 | biostudies-literature | 2003 Jan

REPOSITORIES: biostudies-literature

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Site-specific mutagenesis analysis of PBP 1A from a penicillin-cephalosporin-resistant pneumococcal isolate.

Smith Anthony M AM Klugman Keith P KP

Antimicrobial agents and chemotherapy 20030101 1

Our mutagenesis study has investigated all amino acid mutations in the penicillin-binding domain of PBP 1A from Hungarian pneumococcal isolate 3191 to determine the importance of every mutation in the development of penicillin and cefotaxime resistance. Our data reveal that mutations at amino acid positions 574 to 577 and position 539 cause penicillin and cefotaxime resistance. ...[more]

PMID: 12499220

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Mutations in penicillin-binding protein (PBP) genes and in non-PBP genes during selection of penicillin-resistant Streptococcus gordonii.

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| S-EPMC1693971 | biostudies-literature

Alterations in PBP 1A essential-for high-level penicillin resistance in Streptococcus pneumoniae.

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Validation of β-lactam minimum inhibitory concentration predictions for pneumococcal isolates with newly encountered penicillin binding protein (PBP) sequences.

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2016-02-19 | GSE77436 | GEO

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| S-EPMC6207675 | biostudies-literature

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