Site-specific mutagenesis analysis of PBP 1A from a penicillin-cephalosporin-resistant pneumococcal isolate.
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.
Smith
Anthony M
AM
Respiratory and Meningeal Pathogens Research Unit, Department of Clinical Microbiology and Infectious Diseases, National Health Laboratory Service, Johannesburg, South Africa. anthonys@mail.saimr.wits.ac.za
Klugman
Keith P
KP
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D002352:Carrier Proteins; D018550:Cephalosporin Resistance / Q000235:genetics*; D006602:Hexosyltransferases / Q000235:genetics*; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000235:genetics*; D002267:Muramoylpentapeptide Carboxypeptidase; D016296:Mutagenesis; D010403:Penicillin Resistance / Q000235:genetics*; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases / Q000235:genetics*; D013296:Streptococcus pneumoniae / Q000187:drug effects / Q000235:genetics*
D001426:Bacterial Proteins; D002352:Carrier Proteins; D009097:Multienzyme Complexes; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase