Binding and activation of human plasminogen by Mycobacterium tuberculosis.
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.
Monroy
V
V
Departamento de Biología Molecular, Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México, C.P. 04510 Mexico City D.F., Mexico.
Amador
A
A
Ruiz
B
B
Espinoza-Cueto
P
P
Xolalpa
W
W
Mancilla
R
R
Espitia
C
C
D005337:Fibrin / Q000378:metabolism; D006801:Humans; D066298:In Vitro Techniques; D009169:Mycobacterium tuberculosis / Q000378:metabolism / Q000472:pathogenicity*; D010958:Plasminogen / Q000378:metabolism*; D011485:Protein Binding; D011956:Receptors, Cell Surface / Q000378:metabolism; D055293:Receptors, Urokinase Plasminogen Activator; D014376:Tuberculosis / Q000209:etiology; D000979:alpha-2-Antiplasmin / Q000494:pharmacology
C524898:PLAUR protein, human; D011956:Receptors, Cell Surface; D055293:Receptors, Urokinase Plasminogen Activator; D000979:alpha-2-Antiplasmin; D005337:Fibrin; D010958:Plasminogen