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Publication Abstract from PubMed

Staphylococcus aureus causes a wide range of infections, from mild skin conditions to severe, life-threatening diseases. Bacteriophage endolysins exhibit a selective capacity to degrade the peptidoglycan layer of Gram-positive bacteria, making promising biotherapeutic agents against antibiotic-resistant infections. PlyGRCS, a specific endolysin derived from S. aureus, comprises a catalytic CHAP domain and a cell-wall binding SH3_5 domain connected by a linker. Ca(2+) ions are essential for the CHAP domain's catalytic function. The crystal structure of PlyGRCS, determined in the absence of Ca(2+) and refined to a resolution of 1.67 A, revealed significant conformational changes in the Ca(2+) binding site. Antimicrobial assays with Ca(2+)-deficient PlyGRCS and mutants targeting key residues in the catalytic and Ca(2+) binding regions highlighted the importance of specific functional residues for lytic activity against methicillin-resistant Staphylococcus aureus (MRSA). These structural and microbial studies provide valuable insights into the critical residues contributing to PlyGRCS's bacteriolytic efficacy against MRSA.

Structural Basis for the Essential Role of Ca(2+) in the Lytic Activity of Staphylococcus aureus PlyGRCS Endolysin Targeting Methicillin-Resistant Staphylococcus aureus.,Krishnappa G, Nagaraj H, SureshKumar HB, Mandal M, Padavattan S, Bahubali VH, Thiyagarajan S, Padmanabhan B Proteins. 2024 Dec 11. doi: 10.1002/prot.26777. PMID:39660753^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.