title: Ail proteins of Yersinia pestis and Y. pseudotuberculosis have different cell binding and invasion activities.
abstract: 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.
authors.affiliation: Department of Microbiology and Immunology, University of Michigan School of Medicine Ann Arbor, Michigan, United States of America.
authors.forename: Tiffany M
authors.initials: TM
authors.lastname: Tsang
authors.affiliation: Department of Biomedical and Diagnostic Sciences, University of Detroit Mercy School of Dentistry, Detroit, Michigan, United States of America.
authors.forename: Jeffrey S
authors.initials: JS
authors.lastname: Wiese
authors.affiliation: Department of Biologic and Materials Sciences, University of Michigan School of Dentistry, Ann Arbor, Michigan, United States of America.
authors.forename: Suleyman
authors.initials: S
authors.lastname: Felek
authors.affiliation: Department of Biologic and Materials Sciences, University of Michigan School of Dentistry, Ann Arbor, Michigan, United States of America.
authors.forename: Malte
authors.initials: M
authors.lastname: Kronshage
authors.affiliation: Department of Microbiology and Immunology, University of Michigan School of Medicine Ann Arbor, Michigan, United States of America ; Department of Biomedical and Diagnostic Sciences, University of Detroit Mercy School of Dentistry, Detroit, Michigan, United States of America.
authors.forename: Eric S
authors.initials: ES
authors.lastname: Krukonis
mesh_terms: D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000818:Animals; D001422:Bacterial Adhesion / Q000235:genetics; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002460:Cell Line; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D005353:Fibronectins / Q000378:metabolism; D015870:Gene Expression; D008969:Molecular Sequence Data; D009154:Mutation; D011485:Protein Binding; D055550:Protein Stability; D016415:Sequence Alignment; D037521:Virulence Factors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015010:Yersinia pestis / Q000235:genetics / Q000378:metabolism* / Q000472:pathogenicity; D015011:Yersinia pseudotuberculosis / Q000235:genetics / Q000378:metabolism* / Q000472:pathogenicity
chemical_list: C526543:Ail protein, Yersinia pestis; C576634:Ail protein, Yersinia pseudotuberculosis; D001425:Bacterial Outer Membrane Proteins; D005353:Fibronectins; D037521:Virulence Factors