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

被引:48
作者
Makoveichuk, E
Cherepanov, P
Lundberg, S
Forsberg, Å
Olivecrona, G [1 ]
机构
[1] Umea Univ, Dept Med Biosci, SE-90185 Umea, Sweden
[2] Swedish Def Res Agcy, Div NBC Def, SE-90182 Umea, Sweden
[3] Umea Univ, Dept Mol Biol, SE-90187 Umea, Sweden
关键词
THP-1; macrophages; erythrocytes; liposomes; low density lipoproteins; apolipoprotein B; lipid rafts;
D O I
10.1194/jlr.M200182-JLR200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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-beta-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.
引用
收藏
页码:320 / 330
页数:11
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