An acyl-homoserine lactone acylase found in Stenotrophomonas maltophilia exhibits both quorum quenching activity and the ability to degrade penicillin antibiotics.

ABSTRACT: Stenotrophomonas maltophilia are opportunistic, multi-drug-resistant Gram-negative pathogens increasingly prevalent in clinical settings. Quorum sensing (QS) systems play a crucial role in their pathogenesis, coordinating bacterial populations and enabling interactions within polymicrobial communities. While not the primary QS mechanism in S. maltophilia, these bacteria can respond to acyl-homoserine lactone (AHL)-type autoinducers. Some isolates exhibit AHL-quorum quenching activity, though the responsible components remain unidentified. Homology searches in S. maltophilia K279a revealed a protein with the locus tag SMLT_RS07305 (old locus tag Smlt1522), annotated as a putative penicillin acylase 2 precursor. Sequence and structural analyses classify this protein within the bacterial AHL-

SUBMITTER: Bravo M 

PROVIDER: S-EPMC11903891 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature