Structural, thermodynamic and functional characterization of pneumococcal cell wall hydrolases

Streptococcus pneumoniae is a major cause of morbidity and mortality worldwide. Pneumococcal proteins involved in cell wall hydrolysis (CW hydrolases) are essential for cell expansion and division and contribute in different ways to pneumococcal virulence. In addition, the hydrolases encoded by pneumococcal bacteriophages have emerged as a promising alternative to antibiotics as new antimicrobials. In depth characterization of the bacterial and phage enzymes has provided the first complete structures and models of several family members, clues about substrate specificity and structural motifs recognized by their CW binding domains, and has demonstrated the relevance of modularity for activity. The design of mutants and/or chimeras with different selectivities or enhanced activities has thus been facilitated.

Project partners: Drs. P García and F Díaz (CIB-CSIC); JA Hermoso and M. Bruix (IQFR-CSIC).


Bustamante N, Iglesias-Bexiga M, Bernardo-García N, Silva-Martín N, García G, Campanero-Rhodes MA, García E, Usón I, Buey RM, García P, Hermoso JA, Bruix M, Menéndez M. 2017. Deciphering how Cpl-7 cell wall-binding repeats recognize the bacterial peptidoglycan. Sci Rep. 2017 Nov 28;7(1):16494. doi: 10.1038/s41598-017-16392-4. PMID: 29184076.

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