Virulence factors and drug resistance of gastrointestinal Escherichia coli isolated from different animals

Abstract

Escherichia coli is one of the natural colonizers in the gastrointestinal tract of several animals ranging from terrestrial to aquatic origin. Nowadays virulence attributes of E. coli along with antibiotic resistance pattern is a global crisis. Therefore, it is of utmost importance to monitor the possible virulence characteristics as well as the antibiotic-resistant pattern among the E. coli isolates residing in the gastrointestinal tract of different animals. In this study, a total of 42 E. coli isolates from the gastrointestinal tract of different species like pig, broiler, chicken, fish and goat, as well as from the stool samples of human, were studied for their virulence attributes and antibiotic resistance. Based on the various virulence traits like biofilm-forming, congo red binding, proteolytic, haemolytic, and haemagglutinating activity, this study indicated that 80% of isolates possessed putative factors associated with pathogenicity. Further, these isolates were found to be the extended-spectrum β-lactamase producer and resistant to at least 5 antibiotics, which is a matter of concern since the possibility of horizontal transfer and health implications in the host as well as to human can't be ruled out.

Cleavage of Mucin by Partial Purified Protease Produced from Gastrointestinal Escherichia Coli A29 Isolated from Iraqi Patients

“…In addition to E. coli strains that are harmless commensals found in human gastrointestinal system, there are other strains which are pathogenic E. coli of humans and animals (30) , which classified as those that cause disease inside the gastrointestinal tract and those that can infect outside the gastrointestinal tract (3) . The path type of E. coli has unique pathogenic mechanisms and unique virulence factors that are encoded by particular gene clusters (4) , one of the most important virulence factors is protease activity (5) . Proteases are degradative enzymes that act as a catalyst for protein hydrolysis, have a molecular weight ranging from 18 to 90 KDA.…”