Trypanosoma cruzi calreticulin inhibits the complement lectin pathway activation by direct interaction with L-Ficolin.

Abstract : Trypanosoma cruzi, the agent of Chagas' disease, the sixth neglected tropical disease worldwide, infects 10-12 million people in Latin America. Differently from T. cruzi epimastigotes, trypomastigotes are complement-resistant and infective. CRPs, T-DAF, sialic acid and lipases explain at least part of this resistance. In vitro, T. cruzi calreticulin (TcCRT), a chaperone molecule that translocates from the ER to the parasite surface: (a) Inhibits the human classical complement activation, by interacting with C1, (b) As a consequence, an increase in infectivity is evident and, (c) It inhibits angiogenesis and tumor growth. We report here that TcCRT also binds to the L-Ficolin collagenous portion, thus inhibiting approximately between 35 and 64% of the human complement lectin pathway activation, initiated by L-Ficolin, a property not shared by H-Ficolin. While L-Ficolin binds to 60% of trypomastigotes and to 24% of epimastigotes, 50% of the former and 4% of the latter display TcCRT on their surfaces. Altogether, these data indicate that TcCRT is a parasite inhibitory receptor for Ficolins. The resulting evasive activities, together with the TcCRT capacity to inhibit C1, with a concomitant increase in infectivity, may represent T. cruzi strategies to inhibit important arms of the innate immune response.
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Article dans une revue
Molecular Immunology, Elsevier, 2014, 60 (1), pp.80-5
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http://hal.univ-grenoble-alpes.fr/hal-01097254
Contributeur : Nicole Thielens <>
Soumis le : vendredi 19 décembre 2014 - 11:36:03
Dernière modification le : lundi 19 février 2018 - 14:34:03

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  • HAL Id : hal-01097254, version 1
  • PUBMED : 24769495

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Eduardo Sosoniuk, Gerardo Vallejos, Hany Kenawy, Christine Gaboriaud, Nicole Thielens, et al.. Trypanosoma cruzi calreticulin inhibits the complement lectin pathway activation by direct interaction with L-Ficolin.. Molecular Immunology, Elsevier, 2014, 60 (1), pp.80-5. 〈hal-01097254〉

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