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The  Yersinia pestis  adhesin Ail mediates host cell binding and facilitates delivery of cytotoxic Yop proteins. Ail from  Y. pestis  and  Y. pseudotuberculosis  is identical except for one or two amino acids at positions 43 and 126 depending on the  Y. pseudotuberculosis  strain. Ail from  Y. pseudotuberculosis  strain YPIII has been reported to lack host cell binding ability, thus we sought to determine which amino acid difference(s) are responsible for the difference in cell adhesion.  Y. pseudotuberculosis  YPIII Ail expressed in  Escherichia coli  bound host cells, albeit at ∼50% the capacity of  Y. pestis  Ail.  Y. pestis  Ail single mutants, Ail-E43D and Ail-F126V, both have decreased adhesion and invasion in  E. coli  when compared to wild-type  Y. pestis  Ail.  Y. pseudotuberculosis  YPIII Ail also had decreased binding to the Ail substrate fibronectin, relative to  Y. pestis  Ail in  E. coli . When expressed in  Y. pestis , there was a 30–50% decrease in adhesion and invasion depending on the substitution. Ail-mediated Yop delivery by both  Y. pestis  Ail and  Y. pseudotuberculosis  Ail were similar when expressed in  Y. pestis , with only Ail-F126V giving a statistically significant reduction in Yop delivery of 25%. In contrast to results in  E. coli  and  Y. pestis , expression of Ail in  Y. pseudotuberculosis  led to no measurable adhesion or invasion, suggesting the longer LPS of  Y. pseudotuberculosis  interferes with Ail cell-binding activity. Thus, host context affects the binding activities of Ail and both  Y. pestis  and  Y. pseudotuberculosis  Ail can mediate cell binding, cell invasion and facilitate Yop delivery.

Ail Proteins of Yersinia pestis and Y. pseudotuberculosis Have Different Cell Binding and Invasion Activities