The Psa fimbriae of Yersinia pestis interact with phosphatidylcholine on alveolar epithelial cells and pulmonary surfactant.

The Psa fimbriae of Yersinia pestis interact with phosphatidylcholine on alveolar epithelial cells and pulmonary surfactant. Research Abstract Details 

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The Psa fimbriae of Yersinia pestis interact with phosphatidylcholine on alveolar epithelial cells and pulmonary surfactant. Abstract Text:

Estela M ,Huaiqing Chen,Dieter M Schifferli,

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 muM 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.

The Psa fimbriae of Yersinia pestis interact with phosphatidylcholine on alveolar epithelial cells and pulmonary surfactant. Publishing Authors By Initials

EM ,H Chen,DM Schifferli,

For similar bacteria: gram-negative bacteria: gram-negative facultatively anaerobic rods: enterobacteriaceae: yersinia: yersinia pestis research abstracts see: bacteria: gram-negative bacteria: gram-negative facultatively anaerobic rods: enterobacteriaceae: yersinia: yersinia pestis research

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The Psa fimbriae of Yersinia pestis interact with phosphatidylcholine on alveolar epithelial cells and pulmonary surfactant. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Infection and immunity

VOLUME: 75

Page Numbers: 1272-9

Journal Abbreviation: Infect. Immun.

ISSN: 0019-9567

DAY: 18

MONTH: 12

YEAR: 2006

The Psa fimbriae of Yersinia pestis interact with phosphatidylcholine on alveolar epithelial cells and pulmonary surfactant. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 246127

The Psa fimbriae of Yersinia pestis interact with phosphatidylcholine on alveolar epithelial cells and pulmonary surfactant. Keywords Mesh Terms:

KEYWORDS: Yersinia pestis

MESH TERMS: immunology

Chemical & Substance for Abstract: The Psa fimbriae of Yersinia pestis interact with phosphatidylcholine on alveolar epithelial cells and pulmonary surfactant. Information

Substance Name: pH 6 antigen, Yersinia

Registry Number: 0

Grant and Affiliation Information for The Psa fimbriae of Yersinia pestis interact with phosphatidylcholine on alveolar epithelial cells and pulmonary surfactant.

AFFILIATION: Department of Pathobiology, University of Pennsylvania School of Veterinary Medicine, 3800 Spruce St., Philadelphia, PA 19104, USA.

Country: United States

AGENCY: United States NIAID

GRANT: 1R21 AI053343-01A1

ACRONYM: AI

MEDLINETA: Infect Immun

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