We cloned a 28 kDa outer membrane protein (OMP) of Neisseria meningitidis group B into a live Salmonella typhimurium aroA vaccine strain SL3261. The cloned 28 kDa protein was produced in large amounts in the S. typhimurium transformant SH8182 and located in the outer membrane. A mouse-passaged derivative of SH8182 was used as a live vaccine to immunize mice; with antibiotic pressure the strain survived in the mice as well as the parent strain SL3261 and maintained the plasmid carrying the gene encoding the 28 kDa OMP. The mice produced a high titer of antibodies to the 28 kDa OMP, showing that it had been effectively presented to the immune system. The hyperimmune mouse serum bound in an enzyme immunoassay to whole cells of E. coli and group B meningococci expressing the 28 kDa OMP, but its bactericidal activity towards the meningococci was marginal. In a passive protection study, the antiserum did not protect infant rats from meningococcal infection. The results indicate that the antibodies elicited did not bind to intact meningococcal cells, possibly because of inaccessibility of the 28 kDa OMP.