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首页> 外文期刊>The FEBS journal >Staphylococcus aureus protein A binding to von Willebrand factor A1 domain is mediated by conserved IgG binding regions
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Staphylococcus aureus protein A binding to von Willebrand factor A1 domain is mediated by conserved IgG binding regions

机译：金黄色葡萄球菌蛋白A与von Willebrand因子A1结构域的结合是由保守的IgG结合区介导的

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摘要

Protein A (Spa) is a surface-associated protein of Staphylococcus aureus best known for its ability to bind to the Fc region of IgG. Spa also binds strongly to the Fab region of the immunoglobulins bearing V(H)3 heavy chains and to von Willebrand factor (vWF). Previous studies have suggested that the protein A-vWF interaction is important in S. aureus adherence to platelets under conditions of shear stress. We demonstrate that Spa expression is sufficient for adherence of bacteria to immobilized vWF under low fluid shear. The full length recombinant Ig-binding region of protein A, Spa-EDABC, fused to glutathione-S-transferase (GST), bound recombinant vWF in a dose-dependent and saturable fashion with half maximal binding of about 30 nM in immunosorbent assays. Full length-Spa did not bind recombinant vWF A3 domain but displayed binding to recombinant vWF domains A1 and D'-D3 (half maximal binding at 100 nM and 250 nM, respectively). Each recombinant protein A Ig-binding domain bound to the A1 domain in a similar manner to the full length-Spa molecule (half maximal binding 100 nM). Amino acid substitutions were introduced in the GST-SpaD protein at sites known to be involved in IgG Fc or in V(H)3 Fab binding. Mutants altered in residues that recognized IgG Fc but not those that recognized V(H)3 Fab had reduced binding to vWF A1 and D'-D3. This indicated that both vWF regions recognized a region on helices I and II that overlapped the IgG Fc binding site.
机译：蛋白A（Spa）是金黄色葡萄球菌的表面相关蛋白，以结合IgG Fc区的能力而闻名。 Spa还与带有V（H）3重链的免疫球蛋白的Fab区牢固结合，并与von Willebrand因子（vWF）牢固结合。先前的研究表明，在剪切应力条件下，蛋白A-vWF相互作用对于金黄色葡萄球菌对血小板的粘附至关重要。我们证明，Spa表达足以在低流体剪切力下粘附细菌至固定的vWF。蛋白A的全长重组Ig结合区，Spa-EDABC与谷胱甘肽S-转移酶（GST）融合，以剂量依赖性和饱和方式结合重组vWF，在免疫吸附测定中最大半数结合约为30 nM。全长-Spa不结合重组vWF A3结构域，但是显示出与重组vWF结构域A1和D'-D3的结合（分别在100nM和250nM处有一半最大结合）。每个重组蛋白A Ig结合结构域均以与全长Spa分子相似的方式与A1结构域结合（半最大结合100 nM）。在已知与IgG Fc或V（H）3 Fab结合有关的位点，将GST-SpaD蛋白中的氨基酸取代引入。识别IgG Fc但不识别V（H）3 Fab的残基发生突变的突变体与vWF A1和D'-D3的结合降低。这表明两个vWF区域都识别出螺旋I和II上与IgG Fc结合位点重叠的区域。

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