Characteristics of plasminogen binding to Trypanosoma cruzi epimastigotes

Masyelly Rojas, Indira Labrador, Juan L. Concepción, Elis Aldana, Luisana Avilan*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

The binding constants of the interaction between plasminogen and Trypanosoma cruzi epimastigotes were determined. An indirect method in which the bound plasminogen is detached from the cell by epsilon-aminocaproic acid and a direct method through biotinylated plasminogen were used. The analyses revealed a dissociation constant (Kd) from 0.4 to 1.2microM, these values being compatible with recognition in vivo. Moreover, epimastigotes from the gut of Rhodnius prolixus were able to bind plasminogen from the blood meal. Fragments derived from elastase digestion of plasminogen were tested for their ability to bind T. cruzi cells. The fragment with highest ability to interact with the parasite was miniplasminogen that bound in a concentration-dependent and saturable manner with a Kd similar to that for plasminogen. This binding was inhibited by epsilon-aminocaproic acid indicating that the lysine-binding site of kringle 5 may be responsible for the interaction of plasminogen with T. cruzi.

Original languageEnglish
Pages (from-to)54-58
Number of pages5
JournalActa Tropica
Volume107
Issue number1
Early online date22 Apr 2008
DOIs
Publication statusPublished - Jul 2008

Keywords

  • Animals
  • Binding Sites
  • Humans
  • Kinetics
  • Pancreatic Elastase/metabolism
  • Peptide Fragments/metabolism
  • Plasminogen/metabolism
  • Protein Binding
  • Rhodnius/parasitology
  • Trypanosoma cruzi/isolation & purification

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