作者: Rembert Pieper , Christine L. Gatlin-Bunai , Emmanuel F. Mongodin , Prashanth P. Parmar , Shih-Ting Huang
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摘要: Three isogenic strains derived from a clinical vancomycin-intermediate Staphylococcus aureus isolate were examined by comparative protein abundance analysis. Subcellular fractionation was followed separation in 2-DE gels and spot identification MALDI-TOFTOF-MS LC-MS/MS. Sixty-five significant changes determined. Numerous enzymes participating the purine biosynthesis pathway dramatically increased strain VP32, which featured highest minimal inhibitory concentration for vancomycin, compared to P100 HIP5827. Peptidoglycan hydrolase LytM (LytM) SceD protein, putative transglycosylase, cell envelope fraction of whereas enzyme D-Ala-D-Ala ligase decreased its cytosol fraction. Furthermore, penicillin-binding 2 (PBP2) had substantially higher activity VP32 that LytM, PBP2 catalyze reactions or metabolism wall peptidoglycan. It is plausible expression these are responsible an altered turnover rate, has been observed, peptidoglycan structure, yet be elucidated this highly vancomycin-resistant strain.