Structure, regulation, and host interaction of outer membrane protein U (OmpU) of Vibrio species

Microb Pathog. 2022 Jan:162:105267. doi: 10.1016/j.micpath.2021.105267. Epub 2021 Oct 27.

Abstract

OmpU is a multimeric, cation selective outer membrane protein of Vibrio and related species that non-covalently interact with peptidoglycan layer. Interaction of OmpU with human host cells triggers signaling pathways to promote cytokine secretion, reactive oxygen species production, and caspase independent death in immune and epithelial cells. Non-choleric OmpU imparts resistance to antimicrobial peptides and induces actin cytoskeletal reorganization in the host cells. Further, OmpU isolated from Vibrio species elicits an immune response in several aquaculture hosts. Importantly, in-vivo studies using recombinant OmpU or OmpU derived mimotopes reveal a short-lasting immunity, and protection against Vibrio in the aquaculture sector. In conclusion, OmpU is a key adhesion protein and an important virulence factor for successful colonization of Vibrio species into hosts. This review article provides a broad overview of structural, regulatory, and functional mechanisms of OmpU in normal and disease states.

Keywords: Disease progression; Innate immunity; NFκB; Vaccine; Virulence.

Publication types

  • Review

MeSH terms

  • Adhesins, Bacterial
  • Antimicrobial Peptides
  • Bacterial Outer Membrane Proteins
  • Humans
  • Vibrio Infections* / veterinary
  • Vibrio*

Substances

  • Adhesins, Bacterial
  • Antimicrobial Peptides
  • Bacterial Outer Membrane Proteins