Determination of the activity of the fimF gene and its N-terminal domain disrupted mutant on biofilm formation and its contribution to the oxidative stress response in S. Typhimurium.

SÜRKAÇ, Tuba Nur; AKÇELİK, Nefise; AKÇELİK, Mustafa

Fimbriae is an important virulence factor which plays a key role in cell attachment and colonization of the intestinal mucosa during an infection of Salmonella, a pathogen that causes gastroenteritis and systemic infection in humans. In S. Typhimurium, type 1 fimbriae production strengthens the oxidative stress response. This study aimed to determine the effectiveness of the fimF gene and its N-terminal domain on biofilm formation in S. Typhimurium and their contribution to the oxidative stress response. Before the experiments to prove whether the N-terminal domain of the FimF protein is the region that determines the mechanism and function of the fimF gene; only the N-terminal domain of the fimF gene was cloned behind the pBAD promoter. As a result of biofilm experiments on polystyrene surfaces, it was determined that the biofilm production capacity was reduced significantly in mutant strains in terms of fimF and dam genes (P2O2), it was determined that the mutant strains were more resistant to hydrogen peroxide than the wild-type strain, therefore Salmonella cells perceived the absence of Dam methylase enzyme and FimF protein as a critical internal stress condition and produced strong responses to these stress conditions. As a result of comparative analysis of the N-terminal domain cloned mutant strain with the wild-type, it was proven that the N-terminal domain of the protein in question acts as an adapter protein, due to its close similarities with the wild-type.

SALMONELLA diseases; ADAPTOR proteins; SALMONELLA typhimurium; MOLECULAR cloning; OXIDATIVE stress

Veterinary Journal of Ankara University / Ankara Universitesi Veteriner Fakultesi Dergisi, 2025, Vol 72, Issue 1, p23

1300-0861

Academic Journal

10.33988/auvfd.1390023