PEPTIDOGLYCAN ANALYSIS OF VSE AND VRE

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Enterococcus faecium, an opportunistic pathogen, causes a substantial proportion of enterococcal human infections, particularly in hospitals. Due to the intrinsic resistance that enterococci demonstrate towards many categories of antibiotics (e.g., penicillins), the most successful treatment has been glycopeptides. Glycopeptides cause bacterial cell death by perturbing the integrity of the cell wall. The most powerful glycopeptide, the so-called "drug of last resort," is vancomycin. However, the incidence of infections resistant to vancomycin has increased rapidly since 1988. Solving the problem of enterococcal resistance requires an understanding of the biosynthesis and organization of the cell-wall peptidoglycan, a potential binding site of vancomycin.