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Papers In Press, published online ahead of print November 16, 2002
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Medical Biosciences, Physiological Chemistry, Umeå SE-901 85
Corresponding Author: Gunilla.Olivecrona{at}medbio.umu.se
The bacterial pathogen Yersinia pestis expresses a potential adhesin, the pH6 antigen (pH6-Ag). This appears on the cell surface as polymeric fimbria-like structures after exposure of the bacteria to low pH. The 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 from human plasma, mainly LDL. No interaction between pH6-Ag and HDL could be demonstrated. The binding was not prevented by antibodies against human apoB and was not dependent on the intact structure of apoB. The 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 receptors for LDL on the cell surface. Treatment of the cells with Triton X-100 or with methyl-*-cyclodextrin indicated that the binding of pH6-Ag was partly dependent on lipid rafts. We suggest that the 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 defense systems, and this might be important for the ability of the pathogen to replicate in the susceptible host.
Revised on November 16, 2002
Accepted on November 12, 2002
pH6 antigen of Yersinia pestis interacts with plasma lipoproteins and cell membranes
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