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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  &lt; 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 HIGHLIGHTSLigand 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. 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.

siRNA targeting Atp5a1 gene encoding ATPase α, the ligand of Peg fimbriae, reduced Salmonella Enteritidis adhesion