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Infection and Immunity, October 1998, p. 4965-4970, Vol. 66, No. 10
Division of General Microbiology, Department
of Biosciences, FIN-00014 University of Helsinki,
Finland,1 and
Microbiology and Tumor
Biology Center, Karolinska Institute, 17177 Stockholm,
Sweden2
Received 9 March 1998/Returned for modification 23 April
1998/Accepted 12 July 1998
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
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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
-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.
*
Corresponding author. Mailing address: Division of
General Microbiology, Department of Biosciences, P.O. Box 56 (Viikinkaari 9), FIN-00014 University of Helsinki, Finland. Phone:
358-9-70859260. Fax: 358-9-70859262. E-mail:
timo.korhonen{at}helsinki.fi.
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