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Deciphering how Cpl-7 cell wall-binding repeats recognize the bacterial peptidoglycan

AuthorsBustamante, N.; Iglesias-Bexiga, M.; Bernardo-García, Noelia ; Silva-Martín, Noella; García, G.; Campanero-Rhodes, M. A.; García, Ernesto ; Usón, Isabel ; Buey, Ruben M.; García, Pedro ; Hermoso, Juan A. ; Bruix, M. ; Menéndez, Margarita
Issue Date2017
PublisherNature Publishing Group
CitationScientific Reports 7 (2017)
AbstractEndolysins, the cell wall lytic enzymes encoded by bacteriophages to release the phage progeny, are among the top alternatives to fight against multiresistant pathogenic bacteria; one of the current biggest challenges to global health. Their narrow range of susceptible bacteria relies, primarily, on targeting specific cell-wall receptors through specialized modules. The cell wall-binding domain of Cpl-7 endolysin, made of three CW-7 repeats, accounts for its extended-range of substrates. Using as model system the cell wall-binding domain of Cpl-7, here we describe the molecular basis for the bacterial cell wall recognition by the CW-7 motif, which is widely represented in sequences of cell wall hydrolases. We report the crystal and solution structure of the full-length domain, identify N-acetyl-D-glucosaminyl-(β1,4)-N-acetylmuramyl-L-alanyl-D-isoglutamine (GMDP) as the peptidoglycan (PG) target recognized by the CW-7 motifs, and characterize feasible GMDP-CW-7 contacts. Our data suggest that Cpl-7 cell wall-binding domain might simultaneously bind to three PG chains, and also highlight the potential use of CW-7-containing lysins as novel anti-infectives.
Identifiersdoi: 10.1038/s41598-017-16392-4
issn: 2045-2322
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