ALTERED PENICILLIN-BINDING PROTEINS IN METHICILLIN-RESISTANT STRAINS OF STAPHYLOCOCCUS-AUREUS
ALTERED PENICILLIN-BINDING PROTEINS IN METHICILLIN-RESISTANT STRAINS OF STAPHYLOCOCCUS-AUREUS
复制标题
DOI:
10.1128/aac.19.5.726
复制
发表时间:
1981-01-01
影响因子:
4.9
通讯作者:
TOMASZ, A
中科院分区:
文献类型:
--
作者:
HARTMAN, B;TOMASZ, A
The penicillin-binding proteins (PBP) of a methicillin-resistant (MR) and a methicillin-susceptible (MS) S. aureus were compared by various approaches involving the use of high-specific-activity [3H]penicillin as a reagent. The MR and MS strains were found to contain PBP of the same number and electrophoretic mobilities. Saturation of PBP 1, 2 and 3 by methicillin in the MR strain required the use of several thousands of micrograms of antibiotic/ml; 0.2-0.4 .mu.g of methicillin ml was sufficient to effectively compete with [3H]penicillin for the PBP of the MS strain. Additional experiments indicate that these differences most likely reflect a greatly decreased affinity of the PBP of the MR strain as compared to those of the MS strain. Shift of the pH of the culture medium of the MR strain from pH 7.0-5.2 resulted in an immediate drop in phenotypic resistance to methicillin (from a minimal inhibitory concentration value of 3200 .mu.g/ml at pH 7.0 to 0.8 .mu.g/ml at pH 5.2). Examination of the methicillin affinities of PBP in MR bacteria grown at pH 5.2 showed the presence of the same low-affinity PBP as in bacteria grown at pH 7.0. The pH-dependent resensitization to methicillin cannot be explained by a parallel increase in the antibiotic affinities of the PBP.