Molecular characterization of a monoclonal antibody produced in response to a group C meningococcal polysaccharide peptide mimic.

We have developed a monoclonal antibody, designated anti-anti-Id Ab3-2C4 which reacts with Neisseria meningitidis serogroup C polysaccharide (MCPS). Anti-anti-Id Ab3-2C4 was produced by immunizing Balb/C mice with a peptide mimic of MCPS. This monoclonal antibody reacts with native polysaccharide and its anti-idiotype antibody Ab2-6F9 by ELISA. The synthetic peptide mimic was constructed based on the sequence of the VHCDR3 region of the anti-idiotype Ab2-6F9. We compared the cDNA sequence of Ab3-2C4 to the sequence of idiotype antibody Ab1-1E4 produced in response to native MCPS. The predicted amino acid sequence of the unique VHCDR3 of anti-anti-Id Ab3-2C4 is similar to that of idiotype Ab1-1E4. Also the VHCDR3 of both antibodies is similar to some of the known or suggested carbohydrate binding motifs. A different VH gene family was utilized by Ab3-2C4 than by Ab1-1E4. These results suggest that immunization with the anti-idiotype-derived peptide mimic of the MCPS antigen stimulates the production of antibodies with a binding site structurally related to idiotype antibodies, even though the antibodies Ab1-1E4 and Ab3-2C4 are not related in gene families. Our results support the premise that the use of peptide antigens which are mimics of carbohydrates is an alternate vaccine strategy for polysaccharide antigens and results in an appropriate response.