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Originally published In Press as doi:10.1194/jlr.M200182-JLR200 on November 16, 2002
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 ,
Susanne Lundberg ,
Åke Forsberg , and
Gunilla Olivecrona1,*
* Department of Medical Biosciences, Physiological Chemistry, Umeå University, SE-901 85 Umeå, Sweden
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

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Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.
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