CLONING AND EXPRESSION OF THE NEISSERIA-MENINGITIDIS 5C OUTER-MEMBRANE PROTEIN

The 5C outer membrane protein, one of the N. meningitidis class 5 prot eins, was preferably expressed in bacteria isolated from the nasophary nx and its role in adhering to the mucosal cells and invading them as well as the development of anti-5C antibodies in healthy carriers was demonstrated. Anti-5C monoclonal antibodies are bactericidal in the pr esence of the human complement. The immunodominant region of the 5C pr otein is highly conserved among the different strains of N. meningitid is, and the ope gene, which encodes the protein, does not seem to show antigenic variations. Here the isolation of the ope gene from the Cub an strain B:4:P1.15 by PCR (Polymerase Chain Reaction) is presented. U nder the regulation of the tryptophan promoter, the gene was cloned an d sequenced in E. coli with a high level of expression and fused to th e amino-terminal end of the interleukin-2 gene. In the dot-blot experi ments, the presence of the gene in those strains which did not express the protein in the whole cell ELISA was also detectable.