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

R. Sijbrandi, T. den Blaauwen, J.R.H. Tame, B. Oudega, S. Luirink, B.R. Otto

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

This study describes the identification, cloning and molecular characterization of the α-enolase P46 of Bacteroides fragilis. 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 α-enolase. α-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. © 2004 Elsevier SAS. All rights reserved.
Original languageEnglish
Pages (from-to)9-18
Number of pages10
JournalMicrobes and Infection
Volume7
DOIs
Publication statusPublished - 2005

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