Functional Exposed Amino Acids of LamB as a vaccine candidate for Vibriosis

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.