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Trypanosoma cruzi is lysed by coelomic cytolytic factor-1, an invertebrate analogue of tumor necrosis factor, and induces phenoloxidase activity in the coelomic fluid of Eisenia foetida foetida

par Olivares Fontt, Elizabeth ;Beschin, Alain ;Van Dijck, Els;Vercruysse, Vincent ;Bilej, Martin;Lucas, Rudolf;De Baetselier, Patrick;Vray, Bernard
Référence Developmental and comparative immunology, 26, 1, page (27-34)
Publication Publié, 2002

Article révisé par les pairs

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Résumé :

A cytolytic protein named Coelomic Cytolytic Factor-1 (CCF-1) was isolated from the coelomic fluid of the earthworm Eisenia foetida foetida. Despite the absence of any gene homology, CCF-1 showed functional analogy with the mammalian cytokine tumour necrosis factor (TNF), particularly based on similar lectin-like activity. Indeed, both CCF-1 and TNF recognise N,N′-diacetylchitobiose and exert lytic activity on African Trypanosoma brucei brucei. In this report, we show that South-American Trypanosoma cruzi trypomastigotes, but not epimastigotes, were lysed by earthworm coelomic fluid or purified CCF-1. However, T. cruzi was less susceptible to lysis than T. brucei brucei. This lytic effect of coelomic fluid and CCF-1 on T. cruzi trypomastigotes was partially inhibited in the presence of anti-CCF-1 monoclonal antibody, antibody neutralising the lectin-like activity of TNF or N,N′-diacetylchitobiose. In contrast, this lytic effect was completely inhibited when using T. b. brucei. In addition, T. cruzi components, upon recognition by CCF-1 in E. f. foetida coelomic fluid, triggered the prophenoloxidase cascade, an invertebrate defence mechanism. These results further extend the functional analogies of CCF-1 and TNF, suggesting that both molecules share a similar lectin-like activity that has been conserved as an innate recognition mechanism in invertebrates and vertebrates. They also establish a link between stercorarian (T. cruzi) and salivarian (T. brucei) trypanosomatids having divergent phylogenetic origins and patterns of evolution, but possessing closely related cell surface sugar moieties. © 2001 Elsevier Science Ltd. All rights reserved.