J. Lipid Res. Please sign the JLR Guestbook
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Originally published In Press as doi:10.1194/jlr.M200182-JLR200 on November 16, 2002

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
M200182-JLR200v1
44/2/320    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Makoveichuk, E.
Right arrow Articles by Olivecrona, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Makoveichuk, E.
Right arrow Articles by Olivecrona, G.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?
Journal of Lipid Research, Vol. 44, 320-330, February 2003
Copyright © 2003 by Lipid Research, Inc.

pH6 antigen of Yersinia pestis interacts with plasma lipoproteins and cell membranes

Elena Makoveichuk*, Peter Cherepanov{dagger}, Susanne Lundberg{dagger}, Åke Forsberg{dagger},§ and Gunilla Olivecrona1,*

* Department of Medical Biosciences, Physiological Chemistry, Umeå University, SE-901 85 Umeå, Sweden
{dagger} Department of Medical Countermeasures, Division of NBC-Defense, Swedish Defense Research Agency, SE-901 82 Umeå, Sweden
§ Department of Molecular Biology,, Umeå University, SE-901 87 Umeå, Sweden

1 To whom correspondence should be addressed. e-mail: gunilla.olivecrona{at}medbio.umu.se

The bacterial pathogen Yersinia pestis expresses a potential adhesin, the pH6 antigen (pH6-Ag), which appears as fimbria-like structures after exposure of the bacteria to low pH. pH6-Ag was previously shown to agglutinate erythrocytes and to bind to certain galactocerebrosides. We demonstrate that purified pH6-Ag selectively binds to apolipoprotein B (apoB)-containing lipoproteins in human plasma, mainly LDL. Binding was not prevented by antibodies to apoB. pH6-Ag interacted also with liposomes and with a lipid emulsion, indicating that the lipid moiety of the lipoprotein was responsible for the interaction. Both apoB-containing lipoproteins and liposomes prevented binding of pH6-Ag to THP-I monocyte-derived macrophages as well as pH6-Ag-mediated agglutination of erythrocytes. Binding of pH6-Ag to macrophages was not dependent on the presence of LDL receptors. Treatment of the cells with Triton X-100 or with methyl-ß-cyclodextrin indicated that the binding of pH6-Ag was partly dependent on lipid rafts.

We suggest that interaction of pH6-Ag with apoB-containing lipoproteins could be of importance for the establishment of Y. pestis infections. Binding of lipoproteins to the bacterial surface could prevent recognition of the pathogen by the host defence systems. This might be important for the ability of the pathogen to replicate in the susceptible host.

Abbreviations: apo, apolipoprotein; FC, free cholesterol; MBCD, methyl-ß-cyclodextrin; PC, phosphatidylcholine; pH6-Ag, pH6 antigen; PL, phospholipid; PNGase, peptide N-glycosidase; TC, total cholesterol; TPCK, L-(1-tosylamido-2-phenyl)ethyl chloromethyl ketone

Supplementary key words THP-I macrophages • erythrocytes • liposomes • low density lipoproteins • apolipoprotein B • lipid rafts


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Infect. Immun.Home page
B. Li and R. Yang
Interaction between Yersinia pestis and the Host Immune System
Infect. Immun., May 1, 2008; 76(5): 1804 - 1811.
[Full Text] [PDF]


Home page
Infect. Immun.Home page
K. E. Carlsson, J. Liu, P. J. Edqvist, and M. S. Francis
Influence of the Cpx Extracytoplasmic-Stress-Responsive Pathway on Yersinia sp.-Eukaryotic Cell Contact
Infect. Immun., September 1, 2007; 75(9): 4386 - 4399.
[Abstract] [Full Text] [PDF]


Home page
Infect. Immun.Home page
E. M. Galvan, H. Chen, and D. M. Schifferli
The Psa Fimbriae of Yersinia pestis Interact with Phosphatidylcholine on Alveolar Epithelial Cells and Pulmonary Surfactant
Infect. Immun., March 1, 2007; 75(3): 1272 - 1279.
[Abstract] [Full Text] [PDF]


Home page
Infect. Immun.Home page
B. Li, L. Jiang, Q. Song, J. Yang, Z. Chen, Z. Guo, D. Zhou, Z. Du, Y. Song, J. Wang, et al.
Protein Microarray for Profiling Antibody Responses to Yersinia pestis Live Vaccine
Infect. Immun., June 1, 2005; 73(6): 3734 - 3739.
[Abstract] [Full Text] [PDF]


Home page
Infect. Immun.Home page
X.-Z. Huang and L. E. Lindler
The pH 6 Antigen Is an Antiphagocytic Factor Produced by Yersinia pestis Independent of Yersinia Outer Proteins and Capsule Antigen
Infect. Immun., December 1, 2004; 72(12): 7212 - 7219.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Journal of Biological Chemistry 
 Molecular and Cellular Proteomics   ASBMB Today 
Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.