Immobilization of plasminogen on Escherichia coli flagella.
The interaction of plasminogen with flagella of Escherichia coli was investigated. Plasminogen bound to flagella purified from E. coli LE392, a commonly used cloning host, and E. coli IH3069, an O25H1 strain isolated from a case of newborn bacteremia. The binding was inhibited by the lysine analog epsilon-aminocaproic acid, suggesting involvement of the lysine-binding Kringle domains of plasminogen in the binding. Purified flagella enhanced the formation of plasmin activity in the presence of tissue-type plasminogen activator; a similar enhancement was observed with flagella-expressing LE392 cells.
Lähteenmäki
K
K
Department of General Microbiology, University of Helsinki, Finland.
Westerlund
B
B
Kuusela
P
P
Korhonen
T K
TK
D001665:Binding Sites; D004926:Escherichia coli / Q000378:metabolism* / Q000472:pathogenicity; D005341:Fibrinolysin / Q000378:metabolism; D005407:Flagella / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D010958:Plasminogen / Q000378:metabolism*; D010959:Tissue Plasminogen Activator / Q000378:metabolism; D014774:Virulence / Q000502:physiology
D010958:Plasminogen; D010959:Tissue Plasminogen Activator; D005341:Fibrinolysin