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A licensed <i>Chlamydia trachomatis (Ct)</i> vaccine is not yet available. Recombinant <i>Chlamydia trachomatis</i> major outer membrane protein (<i>Ct</i>-MOMP), the most abundant constituent of the chlamydial outer membrane complex, is considered the most attractive candidate for subunit-based vaccine formulations. Unfortunately, <i>Ct</i>-MOMP is difficult to express in its native structure in the <i>E. coli</i> outer membrane (OM). Here, by co-expression of the Bam complex, we improved the expression and localization of recombinant <i>Ct</i>-MOMP in the <i>E. coli</i> OM. Under these conditions, recombinant <i>Ct</i>-MOMP appeared to assemble into a β-barrel conformation and express domains at the cell surface indicative of correct folding. The data indicate that limited availability of the Bam complex can be a bottleneck for the production of heterologous OM vaccine antigens, information that is also relevant for strategies aimed at producing recombinant OMV-based vaccines.