Salmonella enterica serovar Enteritidis ( S . Enteritidis) is a zoonotic pathogen that can infect both humans and animals. Among the 13 types of fimbrial operons in S . Enteritidis, the highly conserved Peg fimbriae play a crucial role in the adhesion and invasion of S . Enteritidis into host cells but are not well studied. In this study, we identified the ATP synthase subunit alpha (ATPase α) as a ligand of Peg fimbriae using ligand blotting and mass spectrometry techniques. We confirmed the in vitro binding of ATPase α to the purified adhesion protein (PegD). Furthermore, we used siRNA to suppress the expression of ATPase α gene Atp5a1 in Leghorn male hepatoma (LMH) cells, which resulted in a significant reduction in the adhesion rate of S . Enteritidis to the cells ( P < 0.05). The findings in this study provide insight into the mechanism of S . Enteritidis infection through Peg fimbriae and highlight the importance of ATPase α in the adhesion process. RESEARCH HIGHLIGHTS Ligand blotting was performed to screen the ligand of S. Enteritidis Peg fimbriae.Binding assay confirmed that ATPase α is the ligand of the Peg fimbriae.siRNA targeting ATPase α gene ( Atp5a1 ) significantly reduced S . Enteritidis adhesion.
【저자키워드】 siRNA, Salmonella Enteritidis, adhesion, ATPase α, ligand blot, Peg fimbriae,