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Infection and Immunity, March 2007, p. 1272-1279, Vol. 75, No. 3
0019-9567/07/$08.00+0     doi:10.1128/IAI.01153-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

The Psa Fimbriae of Yersinia pestis Interact with Phosphatidylcholine on Alveolar Epithelial Cells and Pulmonary Surfactant{triangledown}

Estela M. Galván, Huaiqing Chen, and Dieter M. Schifferli*

Department of Pathobiology, University of Pennsylvania, School of Veterinary Medicine, Philadelphia, Pennsylvania 19104

Received 23 July 2006/ Returned for modification 5 October 2006/ Accepted 29 November 2006

The pH 6 antigen (Psa) of Yersinia pestis consists of fimbriae with adhesive properties of potential importance for the pathogenesis of plague, including pneumonic plague. The Psa fimbriae mediate bacterial binding to human alveolar epithelial cells. The Psa fimbriae bound mostly to one component present in the total lipid extract from type II alveolar epithelial cells of the cell line A549 separated by thin-layer chromatography (TLC). The Psa receptor was identified as phosphatidylcholine (PC) by TLC using alkali treatment, molybdenum blue staining, and Psa overlays. The Psa fimbriae bound to PC in a dose-dependent manner, and binding was inhibited by phosphorylcholine (ChoP) and choline. Binding inhibition was dose dependent, although only high concentrations of ChoP completely blocked Psa binding to PC. In contrast, less than 1 µM of a ChoP-polylysine polymer inhibited specifically the adhesion of Psa-fimbriated Escherichia coli to PC, and type I (WI-26 VA4) and type II alveolar epithelial cells. These results indicated that the homopolymeric Psa fimbriae are multimeric adhesins. Psa also bound to pulmonary surfactant, which covers the alveolar surface as a product of type II alveolar epithelial cells and includes PC as the major component. The observed dose-dependent interaction of Psa with pulmonary surfactant was blocked by ChoP. Interestingly, surfactant did not inhibit Psa-mediated bacterial binding to alveolar cells, suggesting that both surfactant and cell membrane PC retain Psa-fimbriated bacteria on the alveolar surface. Altogether, the results indicate that Psa uses the ChoP moiety of PC as a receptor to mediate bacterial binding to pulmonary surfactant and alveolar epithelial cells.

* Corresponding author. Mailing address: Department of Pathobiology, University of Pennsylvania School of Veterinary Medicine, 3800 Spruce St., Philadelphia, PA 19104. Phone: (215) 898-1695. Fax: (215) 898-7887. E-mail: dmschiff{at}vet.upenn.edu.

{triangledown} Published ahead of print on 18 December 2006.

Editor: V. J. DiRita

Infection and Immunity, March 2007, p. 1272-1279, Vol. 75, No. 3
0019-9567/07/$08.00+0     doi:10.1128/IAI.01153-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Anisimov, A. P., Bakhteeva, I. V., Panfertsev, E. A., Svetoch, T. E., Kravchenko, T. B., Platonov, M. E., Titareva, G. M., Kombarova, T. I., Ivanov, S. A., Rakin, A. V., Amoako, K. K., Dentovskaya, S. V. (2009). The subcutaneous inoculation of pH 6 antigen mutants of Yersinia pestis does not affect virulence and immune response in mice. J Med Microbiol 58: 26-36 [Abstract] [Full Text]  
  • Galvan, E. M., Lasaro, M. A. S., Schifferli, D. M. (2008). Capsular Antigen Fraction 1 and Pla Modulate the Susceptibility of Yersinia pestis to Pulmonary Antimicrobial Peptides Such as Cathelicidin. Infect. Immun. 76: 1456-1464 [Abstract] [Full Text]  


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