期刊
ACS CHEMICAL BIOLOGY
卷 15, 期 5, 页码 1261-1267出版社
AMER CHEMICAL SOC
DOI: 10.1021/acschembio.0c00002
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-
资金
- [GM124893-01]
Cell walls are barriers found in almost all known bacterial cells. These structures establish a controlled interface between the external environment and vital cellular components. A primary component of cell wall is a highly cross-linked matrix called peptidoglycan (PG). PG cross-linking, carried out by transglycosylases and transpeptidases, is necessary for proper cell wall assembly. Transpeptidases, targets of beta-lactam antibiotics, stitch together two neighboring PG stem peptides (aryl-donor and aryl-acceptor strands). We recently described a novel class of cellular PG probes that were processed exclusively as aryl-donor strands. Herein, we have accessed the other half of the transpeptidase reaction by developing probes that are processed exclusively as aryl-acceptor strands. The critical nature of the cross-bridge on the PG peptide was demonstrated in live bacterial cells, and surprising promiscuity in cross-bridge primary sequence was found in various bacterial species. Additionally, acyl-acceptor probes provided insight into how chemical remodeling of the PG cross-bridge (e.g., amidation) can modulate cross-linking levels, thus establishing a physiological role of PG structural variations. Together, the aryl-donor and -acceptor probes will provide a versatile platform to interrogate PG cross-linking in physiologically relevant settings.
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