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葡萄球菌结合肝素结合型宿主生长因子。

Staphylococci bind heparin-binding host growth factors.

作者信息

Pascu C, Ljungh A, Wadström T

机构信息

Department of Medical Microbiology, University of Lund, Sweden.

出版信息

Curr Microbiol. 1996 Apr;32(4):201-7. doi: 10.1007/s002849900036.

DOI:10.1007/s002849900036
PMID:8867461
Abstract

Staphylococcus aureus, which mediated binding to heparan sulfate, and also strains of coagulase-negative staphylococci (CNS) adhered in high numbers to polymers with end-point attached heparin. A characteristic feature of several cell growth factors is strong affinity for heparin. In the present study, binding of the 125I-labeled heparin-binding growth factors (HBGF), acidic and basic fibroblast growth factor (aFGF, bFGF), and platelet-derived growth factor (PDGF) by S. aureus and CNS strains was examined. Staphylococcal strains used in this study bind bFGF and PDGF, but not aFGF. The binding of bFGF and PDGF was time dependent, influenced by pH and ionic strength for S. aureus Cowan 1. Preincubation of staphylococcal cells with unlabeled bFGF enhanced bFGF binding, but heparin, protamine sulfate, poly-L-lysine, and suramin were potent inhibitors of 125I-bFGF binding to cells of S. aureus Cowan 1. Glycosaminoglycans of comparable size (chondroitin sulfate), other polysulfated polymers (lambda-carrageenan, fucoidan), and some polysulfated polysaccharides (dextran sulfate, pentosan polysulfate) inhibited binding of both GFs to various extents. The partial inhibition of binding of both GFs after protease and periodate treatments indicates that both proteinaceous and other carbohydrate moieties participate in the binding. A lysozyme cell surface extract and bacterial lysates of S. aureus Cowan 1 competitively inhibited binding of 125I-bFGF and 125I-PDGF. These results suggest that staphylococci have the ability to bind two of the HBGFs, bFGF and PDGF, but not aFGF, via more than one cell structure. These binding structures seem to be exposed on the cell surface and deeply anchored in the cytoplasmic membrane as well.

摘要

介导与硫酸乙酰肝素结合的金黄色葡萄球菌以及凝固酶阴性葡萄球菌(CNS)菌株大量黏附于末端连接肝素的聚合物。几种细胞生长因子的一个特征是对肝素有很强的亲和力。在本研究中,检测了金黄色葡萄球菌和CNS菌株对125I标记的肝素结合生长因子(HBGF)、酸性和碱性成纤维细胞生长因子(aFGF、bFGF)以及血小板衍生生长因子(PDGF)的结合情况。本研究中使用的葡萄球菌菌株结合bFGF和PDGF,但不结合aFGF。bFGF和PDGF的结合具有时间依赖性,受金黄色葡萄球菌科恩1型的pH和离子强度影响。用未标记的bFGF对葡萄球菌细胞进行预孵育可增强bFGF的结合,但肝素、硫酸鱼精蛋白、聚-L-赖氨酸和苏拉明是125I-bFGF与金黄色葡萄球菌科恩1型细胞结合的有效抑制剂。大小相当的糖胺聚糖(硫酸软骨素)、其他多硫酸化聚合物(λ-卡拉胶、岩藻依聚糖)以及一些多硫酸化多糖(硫酸葡聚糖、戊聚糖多硫酸盐)在不同程度上抑制了两种生长因子的结合。蛋白酶和高碘酸盐处理后两种生长因子结合的部分抑制表明蛋白质和其他碳水化合物部分都参与了结合。金黄色葡萄球菌科恩1型的溶菌酶细胞表面提取物和细菌裂解物竞争性抑制125I-bFGF和125I-PDGF的结合。这些结果表明葡萄球菌能够通过不止一种细胞结构结合两种HBGF,即bFGF和PDGF,但不结合aFGF。这些结合结构似乎既暴露在细胞表面,也深深锚定在细胞质膜中。

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