Smith Anthony M, Klugman Keith P
Respiratory and Meningeal Pathogens Research Unit, Department of Clinical Microbiology and Infectious Diseases, National Health Laboratory Service, Johannesburg, South Africa.
Antimicrob Agents Chemother. 2003 Jan;47(1):387-9. doi: 10.1128/AAC.47.1.387-389.2003.
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.
我们的诱变研究调查了来自匈牙利肺炎球菌分离株3191的PBP 1A青霉素结合结构域中的所有氨基酸突变,以确定每种突变在青霉素和头孢噻肟耐药性发展中的重要性。我们的数据表明,氨基酸位置574至577以及位置539处的突变会导致对青霉素和头孢噻肟产生耐药性。