Purification and characterization of an immunogenic outer membrane protein of Shigella flexneri 2a.

In the present study we purified 34 kDa major outer membrane protein (MOMP) of Shigella flexneri 2a for the first time, which was cross-reactive and antigenically conserved among Shigella spp. and the epitope was surface exposed on the intact bacterium. The purified antigen was found to be glycosylated, which aids in binding to macrophages and up-regulated the production of nitric oxide, granulocyte-colony stimulating factor and IL-12p70, indicating that the MOMP is immunogenic and has the ability to commence protective immune responses against intracellular pathogens, thereby it may be considered as a potential vaccine candidate.