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Characterization of an iron-regulated alpha-enolase of Bacteroides fragilis

机译：铁调节的脆弱拟杆菌的α-烯醇酶的表征

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摘要

This study describes the identification, cloning and molecular characterization of the a-enolase P46 of Bacteroides flagilis. The Gram-negative anaerobic bacterium B. fragilis is a member of the commensal flora of the human intestine but is also frequently found in severe intra-abdominal infections. Several virulence factors have been described that may be involved in the development of these infections. Many of these virulence factors are upregulated under conditions of iron- or heme-starvation. We found a major protein of 46 kDa (P46) that is upregulated under iron-depleted conditions. This protein was identified as an alpha-enolase. alpha-Enolases in several Gram-positive bacteria and eukaryotic cells are located at the cell surface and function as plasminogen-binding proteins. Localization studies demonstrated that P46 is mainly located in the cytoplasm and partly associated with the inner membrane (IM). Under iron-restricted conditions, however, P46 is localized primarily in the IM fraction. Plasminogen-binding to B. fragilis cells did occur but was not P46 dependent. A 60-kDa protein was identified as a putative plasminogen-binding protein in B. fragilis. (C) 2004 Elsevier SAS. All rights reserved.
机译：这项研究描述了鞭毛拟杆菌的α-烯醇酶P46的鉴定，克隆和分子表征。脆弱的革兰氏阴性厌氧菌是人肠道共生菌群的成员，但也经常在严重的腹腔内感染中发现。已经描述了可能与这些感染的发展有关的几种毒力因子。在铁或血红素饥饿的条件下，许多毒力因子被上调。我们发现46 kDa（P46）的主要蛋白质在铁耗尽的条件下上调。该蛋白被鉴定为α-烯醇酶。几种革兰氏阳性细菌和真核细胞中的α-烯醇酶位于细胞表面，并起纤溶酶原结合蛋白的作用。定位研究表明，P46主要位于细胞质中，部分与内膜（IM）相关。但是，在铁限制条件下，P46主要位于IM部分。确实发生了纤溶酶原结合脆弱性芽孢杆菌细胞，但不是P46依赖性的。 60 kDa的蛋白质被确定为脆弱的B. gillis中的纤溶酶原结合蛋白。 （C）2004 Elsevier SAS。版权所有。

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