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Outer membrane protein A (OmpA) is a major, highly conserved protein located in the outer membrane of Shigella species, such as S. flexneri [PMID: 11004100]. It plays a fundamental role in maintaining the structural integrity of the bacterial cell envelope by anchoring the outer membrane to the underlying peptidoglycan layer [UniProt: P0A910]. Beyond its structural importance, OmpA is a critical virulence factor that facilitates the adhesion of Shigella to host intestinal epithelial cells, which is a prerequisite for bacterial invasion and the development of shigellosis (bacillary dysentery) [PMID: 25691594]. OmpA also functions as a porin for the passage of small solutes and is involved in biofilm formation and resistance to host innate immune defenses [PMID: 30639145]. Because it is surface-exposed and highly conserved across various serotypes, OmpA is a primary target for the development of subunit vaccines and novel antimicrobial strategies [PMID: 15575015]. Current therapeutic research focuses on using OmpA as an antigen to elicit protective immune responses or developing inhibitors that disrupt its role in host cell attachment [PMID: 28438978].
Induction of neutralizing antibodies and inhibition of bacterial adhesion to host epithelial cells.
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