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首页> 外文期刊>FEMS Microbiology Letters >Analysis of the expression of the putatively virulence-associated neisserial protein RmpM (class 4) in commensal Neisseria and Moraxella catarrhalis strains
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Analysis of the expression of the putatively virulence-associated neisserial protein RmpM (class 4) in commensal Neisseria and Moraxella catarrhalis strains

机译:推定的与毒力相关的奈瑟球菌蛋白RmpM(4类)在共生奈瑟菌和卡他莫拉菌菌株中的表达分析

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摘要

The RmpM protein has been reported to be present only in pathogenic Neisseria species. In the present study we demonstrate that this protein is also present at least in N. lactamica and N. sicca strains. The N. lactamica protein reacts with a RmpM-specific monoclonal antibody (185,H-8), having a molecular mass (similar to 31 kDa) slightly lower than that of the meningococcal RmpM, and mouse antibodies from sera against outer membrane vesicles from both N. lactamica and N. sicca strains cross-react with the meningococcal RmpM. PCR and hybridization experiments with a complete rmpM probe agree with the immunodetection experiments. Our results strongly suggest that the meningococcal RmpM should not be considered a virulence marker, and the presence of this protein in the commensal species agrees with its role as a structural protein, proposed for the RmpM. which should be considerably conserved in the,Neisseria species. (C) 2001 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved. [References: 19]
机译:据报道,RmpM蛋白仅存在于致病性奈瑟氏菌中。在本研究中,我们证明了这种蛋白质至少也存在于乳酸奈瑟菌和干燥奈瑟菌中。乳酸奈瑟球菌蛋白与RmpM特异性单克隆抗体(185,H-8)反应,其分子质量(约31 kDa)略低于脑膜炎球菌RmpM的分子量,而小鼠抗体则来自血清中的抗外膜小泡乳酸奈瑟菌和干燥双歧杆菌均与脑膜炎球菌RmpM交叉反应。具有完整rmpM探针的PCR和杂交实验与免疫检测实验一致。我们的研究结果强烈表明,不应将脑膜炎球菌RmpM视为一种毒性标记物,该蛋白在共生物种中的存在与其作为RmpM提出的结构蛋白的作用相吻合。在奈瑟氏球菌属中应保守得多。 (C)2001年欧洲微生物学会联合会。由Elsevier Science B.V.保留所有权利。 [参考:19]

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