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Título

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

AutorBustamante, Noemí CSIC; Iglesias-Bexiga, Manuel CSIC; Bernardo-García, Noelia CSIC; Silva-Martín, Noella CSIC; García, Guadalupe CSIC; Campanero-Rhodes, María Asunción CSIC ORCID; García, Ernesto CSIC ORCID ; Usón, Isabel CSIC ORCID ; Martínez Buey, Rubén CSIC ORCID; García, Pedro CSIC ORCID ; Hermoso, Juan A. CSIC ORCID; Bruix, M. CSIC ORCID ; Menéndez, Margarita CSIC ORCID
Fecha de publicación2017
EditorNature Publishing Group
CitaciónScientific Reports 7 (2017)
ResumenEndolysins, 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.
URIhttp://hdl.handle.net/10261/162271
DOI10.1038/s41598-017-16392-4
Identificadoresdoi: 10.1038/s41598-017-16392-4
issn: 2045-2322
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