Functional Exposed Amino Acids of OpcA as a vaccine candidate for Neisseria meningitidis

Neisseria meningitidis, a human-specific pathogen, is a gram-negative, aerobic, non endospore forming diplococcus of the Proteobacteria phylum. This nonmotile, yet piliated bacterium is enveloped with a carbohydrate capsule that is covered with and distinguished by the polysaccharides attached to its surface, and is targeted by the host's immune system. The OpcA family of outer membrane proteins is a group surface-exposed and porinproteins that are in high-copy number in the outer membrane of mainly Gram-negative bacteria. Porins typically control the diffusion of small metabolites like sugars, ions, and amino acids.Findings indicated that antibodies against OpcA were protective, making this antigen a likely candidate for a vaccine. Early clinical trials demonstrated that recombinant OpcA was immunogenic and well tolerated, even in subjects with a history of Neisseria meningitidisdisease.The present study was designed to resolving the major obstacles in the control or in prevention of Neisseria meningitidis disease. We exploited bioinformatic tools to better understanding and characterizing the OpcA structure and select appropriate regions as effectiveB cell epitops.

Keywords:

B cell epitops , Neisseria meningitidis , OpcA , Bioinformatic