Abstract
Edwardsiellosis caused by Edwardsiella tarda and Edwardsiella piscicida is one of the most common catfish diseases. For any bacterium to cause an infection, it has to adhere to and invade the host. Major fimbrial protein (fimA) plays an important role in the adherence of Edwarsiella spp. using an in-silico approach, physicochemical properties, secondary structure, functional properties and homology modelling of fimA protein from E. tarda and E. piscicida were analysed in this study. The primary structural analysis indicated that all proteins are soluble, stable and hydrophobic. Secondary structures analysed using the SOPMA tool revealed that extended strands, random coils and alpha helices are predominant amidst secondary structural elements. The homology models of these proteins were built using SWISS-MODEL and their qualities were validated using ProSA, ProQ, PROCHECK and RAMPAGE analysis. The validated models were verified as good structures. The results suggested that the fimA can be a potential target for diagnosis and drug development to combat edwardsiellosis infection.
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