NagPIBAF upregulation and ompO downregulation compromise oxidative stress tolerance of Stenotrophomonas maltophilia.

ABSTRACT:

Background

Outer membrane protein OmpA is composed of two domains, an N-terminal β-barrel structure embedded in the outer membrane and a C-terminal globular domain noncovalently associated with the peptidoglycan layer in periplasm. Stenotrophomonas maltophilia KJ is a clinical isolate. In our recent study, we disclosed that KJ∆OmpA_{299 - 356,} an OmpA C-terminal deletion mutant, compromised menadione tolerance. Furthermore, the involvement of σ^E, σ^N, and ompO in the ∆ompA_{299 - 356}-mediated phenotype was proposed. In that study, we hypothesized that there was an unidentified σ^N-regulated candidate responsible for ∆ompA_{299 - 356}-mediated menadione tolerance decrease, and the candidate was disclosed in this study.

Meth

SUBMITTER: Yang TC 

PROVIDER: S-EPMC11887185 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature