Summary

The main objective of this line of research is the cloning and expression in E. coli bacteria of the outer membrane transport proteins of the Fe(III) siderophore complexes of pathogenic bacteria in aquaculture fish, and their subsequent purification to obtain the corresponding recombinant protein for use as an antigen for testing as a vaccine against infectious diseases caused by these bacteria. Additionally, the three-dimensional structure of this recombinant protein is determined by X-ray crystallography, which can be of great help in the design of conjugates for testing as antimicrobials against infectious diseases in aquaculture fish.

Following this scheme, it was possible to clone and express the outer membrane transport protein FrpA, involved in the recognition, reception, and subsequent transport of the Fe(III) siderophore complex piscibactin, in E. coli bacteria. Its purification allowed the isolation of its corresponding recombinant protein rFpA. Its subsequent use as an antigen for testing as a vaccine against photobacteriosis showed a high degree of protection.