Unraveling the Virulence Factors and Secreted Proteins of an Environmental Isolate Enterobacter sp. S-16.

Abstract

Members of the Enterobacter genus include many pathogenic microbes of humans and plants, secrete proteins that contribute to the interactions of bacteria and their environment. Therefore, understanding of secreted proteins is vital to understand bacterial physiology and behavior. Here, we explored the secretome of an environmental isolate Enterobacter sp. S-16 by nanoLC-MS/MS and identified 572 proteins in the culture supernatant. Gene ontology (GO) analysis indicated that proteins were related to biological processes, molecular as well as cellular functions. The majority of the identified proteins are involved in microbial metabolism, chemotaxis & motility, flagellar hook-associated proteins, biosynthesis of antibiotics, and molecular chaperones to assist the protein folding. Bioinformatics analysis of the secretome revealed the presence of type I and type VI secretion system proteins. Presence of these diverse secretion system proteins in Enterobacter sp. S-16 are likely to be involved in the transport of various proteins including nutrient acquisition, adhesion, colonization, and homeostasis maintenance. Among the secreted bacterial proteins with industrial importance, lignocellulolytic enzymes play a major role, therefore, we analyzed our secretome results for any presence of glycoside hydrolases (GHs) and other hydrolytic enzymes (CAZymes). Overall, the secreted proteins may be considered an attractive reservoir of potential antigens for drug development, diagnostic markers, and other biomedical applications.