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Vibrio cholerae O1 organisms belonging to different biotypes and serotypes were shown to express major outer membrane proteins (MOMPs) with subunit molecular masses of 48 to 50, 40 to 43, 35 to 36, 27 to 28, and 20 kDa. Antisera raised against individual MOMPs of a V. cholerae O1 strain recognized MOMPs of corresponding molecular masses in other O1 and non-O1 strains. Serological data also suggested possible differences in the cell surface exposition of these MOMPs. However, no marked differences between V. cholerae cells grown in vitro and in vivo could be noted in respect to the expression or surface exposition of these MOMPs. Of five MOMPs studied in this work, 40- to 43- and 20-kDa cell surface proteins were shown to be of considerable importance, as antisera to these proteins induced significant protection against V. cholerae challenge in the suckling mouse model. Similar protection, although to a lesser extent, was demonstrable with the antiserum to the 27- to 28-kDa protein. These results were corroborated with the Fab (immunoglobulin G) [Fab(IgG)] fragments of the antisera, thereby suggesting that the observed protection induced by anti-MOMP antibodies did not arise as a result of bacterial clumping. Subsequent studies demonstrated that these antisera as well as their Fab (IgG) fragments induced significant inhibition of intestinal colonization of V. cholerae. The 40- to 43- and 27- to 28-kDa proteins appeared to be porinlike, while the 20-kDa protein was found to be antigenically related to TcpA (subunit A of toxin-coregulated pilus). All these results demonstrate the involvement of more than one cell surface antigen of V. cholerae in the induction of protective immunity through inhibition of intestinal colonization of vibrios.

Major outer membrane proteins of Vibrio cholerae and their role in induction of protective immunity through inhibition of intestinal colonization