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首页> 外文期刊>Infection and immunity >Monoclonal antibodies that recognize a common pneumococcal protein with similarities to streptococcal group A surface glyceraldehyde-3-phosphate dehydrogenase.
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Monoclonal antibodies that recognize a common pneumococcal protein with similarities to streptococcal group A surface glyceraldehyde-3-phosphate dehydrogenase.

机译:识别与肺炎球菌A组表面甘油醛-3-磷酸脱氢酶相似的常见肺炎球菌蛋白的单克隆抗体。

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Monoclonal antibodies (MAbs) against clinical isolates of Streptococcus pneumoniae were produced in a search for common pneumococcal proteins. One of the fusions generated two MAbs, 174,B-8 (immunoglobulin G2a) and 177,D-8 (immunoglobulin G1), which by Western blotting (immunoblotting) stained with a main band of 40 kDa found in all isolates of S. pneumoniae examined. Cross-reactivity studies with streptococci other than pneumococci revealed very weak or moderate reactions with the MAbs. The 40-kDa protein was isolated by immunoaffinity chromatography and subsequent preparative Western blotting. N-terminal amino acid sequencing showed 90% amino acid sequence homology with a surface-located glyceraldehyde-3-phosphate dehydrogenase from Streptococcus pyogenes. This protein has also been reported to exhibit binding to mammalian proteins such as fibronectin, which may serve as host receptors. The epitopes for MAbs 174,B-8 and 177,D-8 reacting with the pneumococcal analog were not accessible to antibody binding in live bacteria but were exposed after heat killing. The MAbs showed negligible cross-reactions with S. pyogenes.
机译:为了寻找常见的肺炎球菌蛋白,产生了针对肺炎链球菌临床分离株的单克隆抗体(MAb)。融合体之一产生了两个单克隆抗体,分别为174,B-8(免疫球蛋白G2a)和177,D-8(免疫球蛋白G1),通过Western印迹(免疫印迹)将其在所有S分离株中发现的40 kDa主带染色。检查了肺炎。与除肺炎球菌以外的链球菌的交叉反应研究表明,与单克隆抗体的反应非常弱或中等。通过免疫亲和层析和随后的制备性蛋白质印迹分离40-kDa蛋白。 N末端氨基酸测序显示与化脓性链球菌表面定位的甘油醛-3-磷酸脱氢酶具有90%的氨基酸序列同源性。还已经报道该蛋白表现出与诸如纤连蛋白的哺乳动物蛋白的结合,其可以用作宿主受体。与肺炎球菌类似物反应的单克隆抗体174,B-8和177,D-8的表位无法与活细菌中的抗体结合,但在热杀死后暴露。 MAb与化脓性链球菌的交叉反应可忽略不计。

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