functional exposed amino acids of lamB as a vaccine candidate for vibriosis

elahe dehghani ashkezari¹ fateme sefid²

1) departmant of biology ,art and science university of yazd ,
2) departmant of biology ,shahed university ,tehran-qom express

Publication : 3rd international conference of Science and Engineering(3icesconf.com)
Abstract :
Vibriosis is one of the most serious infectious diseases in fish and shellfish. However, due to the diversity of pathogens and their complicated serotypes, the progress in vaccine development against Vibriosis has been slow. LamB proteins (or maltoporins) are a family of OMPs. It forms a betabarrel composed of three monomers and ensures the transport of maltose and maltodextrin in Gram-negative bacteria reported that recombinant Aeromonas hydrophila outer membrane protein 48, which belongs to the maltoporin group of porins, induces a protective immune response against A. hydrophila and E. tarda. Findings indicated that antibodies against LamB were protective, making this antigen a likely candidate for a vaccine. Early clinical trials demonstrated that recombinant LamB was immunogenic and well tolerated, even in subjects with a history of vibrio disease. The present study was designed to in silico resolving the major obstacles in the control or in prevention of vibrio diseases. We exploited bioinformatic tools to better understanding and characterizing the LamB structure and select appropriate regions as effective B cell epitops.
Keywords : B cell epitops LamB Outer surface proteins Vibriosis