Identification of two laminin-binding fimbriae, the type 1 fimbria of Salmonella enterica serovar typhimurium and the G fimbria of Escherichia coli, as plasminogen receptors.
Escherichia coli strains carrying recombinant plasmids encoding either the type 1 fimbria of Salmonella enterica serovar Typhimurium or the G fimbria of E. coli exhibited binding of human 125I-Glu-plasminogen and enhanced the tissue-type plasminogen activator-catalyzed conversion of plasminogen to plasmin. Purified type 1 or G fimbriae similarly bound plasminogen and enhanced its activation. The binding of plasminogen did not involve the characteristic carbohydrate-binding property of the fimbriae but was inhibited at low concentrations by the lysine analog epsilon-aminocaproic acid. Because these fimbrial types bind to laminin of basement membranes (M. Kukkonen et al., Mol. Microbiol. 7:229-237, 1993; S. Saarela et al., Infect. Immun. 64:2857-2860, 1996), the results demonstrate a structural unity in the creation and targeting of bacterium-bound proteolytic plasmin activity to basement membranes.
Kukkonen
M
M
Division of General Microbiology, Department of Biosciences, FIN-00014 University of Helsinki, Finland.
Saarela
S
S
Lähteenmäki
K
K
Hynönen
U
U
Westerlund-Wikström
B
B
Rhen
M
M
Korhonen
T K
TK
D015119:Aminocaproic Acid / Q000494:pharmacology; D004926:Escherichia coli / Q000378:metabolism*; D005341:Fibrinolysin / Q000378:metabolism; D010861:Fimbriae, Bacterial / Q000378:metabolism*; D006801:Humans; D010958:Plasminogen / Q000378:metabolism*; D011485:Protein Binding / Q000187:drug effects; D011956:Receptors, Cell Surface / Q000378:metabolism*; D055293:Receptors, Urokinase Plasminogen Activator; D012486:Salmonella typhimurium / Q000378:metabolism*; D010959:Tissue Plasminogen Activator / Q000378:metabolism
C524898:PLAUR protein, human; D011956:Receptors, Cell Surface; D055293:Receptors, Urokinase Plasminogen Activator; D010958:Plasminogen; D010959:Tissue Plasminogen Activator; D005341:Fibrinolysin; D015119:Aminocaproic Acid