Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 54, Issue 36, Pages 10492-10496Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201503869
Keywords
bacteria; biosensors; crosslinking; fluorescent probes; peptidoglycans
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Funding
- Camille and Henry Dreyfus Foundation
- Novartis
- Alfred P. Sloan Foundation [BR2011-117]
- NIH [1DP2OD002913-01]
- NIH MSTP [T32GM07205]
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Penicillin-binding proteins (PBPs) catalyze the crosslinking of peptidoglycan (PG), an essential process for bacterial growth and survival, and a common antibiotic target. Yet, despite its importance, little is known about the spatiotemporal aspects of crosslinkinglargely because of a lack of experimental tools for studying the reaction in live bacteria. Here we introduce such a tool: an activity-based probe that enables visualization and relative quantitation of crosslinking in vivo. In Staphylococcus aureus, we show that fluorescent mimics of the natural substrate of PBPs (PG stem peptide) are covalently incorporated into the cell wall, installing fluorophores in place of natural crosslinks. These fluorescent stem peptide mimics (FSPMs) are selectively recognized by a single PBP in S. aureus: PBP4. Thus, we were able to use FSPM pulse-labeling to localize PBP4 activity in live cells, showing that it is recruited to the septum in a manner dependent on wall teichoic acid.
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