A Periplasmic Antimicrobial Peptide-Binding Protein Is Required for Stress Survival in Vibrio cholerae

Frontiers in Microbiology
Jessica Saul-McBeth, Jyl S Matson

Abstract

Vibrio cholerae must sense and respond appropriately to stresses encountered in the aquatic environment and the human host. One stress encountered in both environments is exposure to antimicrobial peptides (AMPs), produced as a part of the innate immune response by all multicellular organisms. Previous transcriptomic analysis demonstrated that expression of Stress-inducible protein A (SipA) (VCA0732), a hypothetical protein, was highly induced by AMP exposure and was dependent on a specific uncharacterized two-component system. In order to better understand role of this protein in stress relief, we examined whether it shared any of the phenotypes reported for its homologs. SipA is required for survival in the presence of two other stressors, cadmium chloride and hydrogen peroxide, and it localizes to the bacterial periplasm, similar to its homologs. We also found that SipA physically interacts with OmpA. Importantly, we found that SipA binds AMPs in the bacterial periplasm. This suggests a model where SipA may act as a molecular chaperone, binding AMPs that enter the periplasm and delivering them to OmpA for removal from the cell. While El Tor V. cholerae strains lacking SipA do not show a survival defect in the presence of AMP...Continue Reading

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Citations

Oct 13, 2020·Frontiers in Immunology·Souwelimatou Amadou Amani, Mark L Lang
Nov 17, 2020·Frontiers in Cellular and Infection Microbiology·Zixin QinZhi Liu

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Methods Mentioned

BETA
RNA-Seq
PCR
coimmunoprecipitation
enzyme-linked immunosorbent assay

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