BACTERIAL-RESISTANCE TO COMPLEMENT KILLING MEDIATED BY THE AIL PROTEIN OF YERSINIA-ENTEROCOLITICA

Ail is a 17-kDa outer membrane Yersinia protein that mediates bacterial attachment to, and invasion of, cultured epithelial cells. We report here an alternative role for Ail in the pathogenesis of Yersinia infection. We found that Escherichia coli HB101 harboring the 4-kilobase recombinant ail clone pVM102 were highly resistant to killing in up to 50% normal human serum. A 674-base-pair fragment of DNA from pVM102, which encodes the ail gene, was inserted into pUC18 and shown to promote full resistance to complement killing in E. coli HB101. Cellular attachment and resistance to complement killing in a plasmid-cured inv- strain of Yersinia enterocolitica (0:8) was correlated with the thermoinduced expression of Ail at 37-degrees-C. Insertional inactivation of ail in Y. enterocolitica resulted in loss of both thermoinduced bacterial properties. Cellular attachment and serum resistance were restored by complementation of the defect by plasmid-encoded ail. Complementation of cell attachment activity required bacterial growth at 37-degrees-C, indicating that an additional thermoinduced factor is required for this Ail function. In addition, these studies reveal that functional homology exists between Ail and the structurally related protein Rck, which promotes resistance to complement killing in Salmonella typhimurium.