Vibrio cholerae O1 Inaba outer-membrane surface protein antigens (Vc O1 Inaba OMP)

Vibrio cholerae O1 Inaba outer-membrane surface protein antigens are a group of immunogenic proteins located on the external surface of the Inaba serotype of Vibrio cholerae O1, the primary cause of epidemic cholera (NIH, 2021; MDPI, 2021). This protein family includes major outer membrane proteins (OMPs) such as OmpU, OmpT, and OmpW, as well as the toxin-coregulated pilus (TCP) subunit TcpA, which are essential for the pathogen's survival and virulence (Wikipedia; NIH, 1998). OmpU and OmpT function as porins that regulate nutrient influx and protect the bacteria from host-derived stressors like bile salts, while TCP is the primary adhesin required for colonizing the human small intestine (Journal of Biological Chemistry, 2003; NIH, 2024). In the context of disease, these surface antigens are the primary targets for the host's adaptive immune response, particularly the production of vibriocidal antibodies that correlate with protection (Infection and Immunity, 2004; MDPI, 2019). Vaccines such as Dukoral, Shanchol, and Vaxchora utilize these antigens—either as part of killed whole cells or in live attenuated strains—to induce protective mucosal and systemic immunity (NIH, 1990; SCIRP, 2010). By targeting these proteins, the immune system can effectively block bacterial colonization and the subsequent secretion of cholera toxin, which causes the severe, life-threatening diarrhea characteristic of the disease (NIH, 1992; ASM, 1992). However, challenges such as serotype switching between Inaba and Ogawa and the limited duration of immunity in young children remain significant considerations for vaccine efficacy (Oxford University Press, 2014).

Other names

Vibrio cholerae O1 Inaba outer-membrane surface protein antigensV. cholerae O1 Inaba OMPsInaba major outer membrane proteinsInaba surface antigensVibrio cholerae O1 Inaba MOMPs

Vaccine-mediated induction of vibriocidal and anti-colonization antibodies that target surface antigens to prevent bacterial attachment, promote complement-mediated lysis, and inhibit intestinal colonization.