α-Enolase binds to human plasminogen on the surface of Bacillus anthracis

被引：81

作者：

Agarwal, Shivangi ^{[1
]}

Kulshreshtha, Parul ^{[1
]}

Mukku, Dhananjay Bambah ^{[2
]}

Bhatnagar, Rakesh ^{[1
]}

机构：

[1] Jawaharlal Nehru Univ, Sch Biotechnol, Lab Mol Biol & Genet Engn, New Delhi 110067, India

[2] Mt Sinai Sch Med, Fishberg Dept Neurosci, New York, NY 10029 USA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS | 2008年 / 1784卷 / 7-8期

关键词：

alpha-enolase; extracellular matrix proteins; plasminogen; fibrinolysis; flow cytometry;

D O I：

10.1016/j.bbapap.2008.03.017

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

alpha-enolase of Bacillus anthracis has recently been classified as an immunodominant antigen and a potent virulence factor determinant. alpha-enolase (2-phospho-D-glycerate hydrolase (EC 4.2.1.11), a key glycolytic metalloenzyme catalyzes the dehydration of D-(+)-2-phosphoglyceric acid to phosphoenolpyruvate. Interaction of surface bound alpha-enolase with plasminogen has been incriminated in tissue invasion for pathogenesis. B. anthracis alpha-enolase was expressed in Escherichia coli and the recombinant enzyme was purified to homogeneity that exhibited a K-m of 3.3 mM for phosphoenolpyruvate and a V-max of 0.506 mu Mmin(-1) mg(-1). B. anthracis whole cells and membrane vesicles probed with anti-enolase antibodies confirmed the surface localization of alpha-enolase. The specific interaction of a.-enolase with human plasminogen (but not plasmin) evident from ELISA and the retardation in the native gel reinforced its role in plasminogen binding. Putative plasminogen receptors in B. anthracis other than enolase were also observed. This binding was found to be carboxypeptidase sensitive implicating the role of C-terminal lysine residues. The recombinant enolase displayed in vitro laminin binding, an important mammalian extracellular matrix protein. Plasminogen interaction conferred B. anthracis with a potential to in vitro degrade fibronectin and exhibit fibrinolytic phenotype. Therefore, by virtue of its interaction to host plasminogen and extracellular matrix proteins, alpha-enolase may contribute in augmenting the invasive potential of B. anthracis. (C) 2008 Elsevier B.V. All rights reserved.

引用

页码：986 / 994

页数：9

共 35 条

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