Abstract
The first evidence of the interaction of Mycobacterium tuberculosis with the plasminogen system is herein reported. By FACScan analysis and affinity blotting, lysine-dependent binding of plasminogen to M. tuberculosis was demonstrated. The binding molecules were 30-, 60-, and 66-kDa proteins present in cell wall and soluble protein extracts. The activation of plasminogen, which occurred only in presence of fibrin and was not inhibited by the host serpin, alpha(2)-antiplasmin, was also demonstrated.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Fibrin / metabolism
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Humans
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In Vitro Techniques
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Mycobacterium tuberculosis / metabolism
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Mycobacterium tuberculosis / pathogenicity*
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Plasminogen / metabolism*
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Protein Binding
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Receptors, Cell Surface / metabolism
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Receptors, Urokinase Plasminogen Activator
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Tuberculosis / etiology
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alpha-2-Antiplasmin / pharmacology
Substances
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PLAUR protein, human
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Receptors, Cell Surface
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Receptors, Urokinase Plasminogen Activator
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alpha-2-Antiplasmin
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Fibrin
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Plasminogen