Trypanosoma cruzi 175-kDa protein tyrosine phosphorylation is associated with host cell invasion

Trypanosoma cruzi 175-kDa protein tyrosine phosphorylation is associated with host cell invasion

Autor Favoreto, S. Google Scholar
Dorta, M. L. Google Scholar
Yoshida, N. Google Scholar
Instituição Universidade Federal de São Paulo (UNIFESP)
Resumo We examined the requirement of Trypanosoma cruzi protein tyrosine phosphorylation for parasite entry into mammalian cells and analyzed the profile of phosphorylated proteins in infective trypomastigotes. Treatment of metacyclic or tissue culture trypomastigotes with genistein, an inhibitor of protein tyrosine kinase activity, significantly inhibited invasion of cultured HeLa cells. A soluble factor, contained in HeLa cell extract and absent in the extract or T. cruzi-resistant K562 cells, greatly enhanced phosphorylation levels of a 175-kDa protein (p175) in trypomastigotes. Genistein inhibited p175 tyrosine phosphorylation. P175 was undetectable in noninvasive epimastigotes. the phosphorylation-inducing activity of HeLa cell extract was abrogated by adsorption with metacyclic trypomastigotes but not with epimastigotes or when it was mixed with recombinant protein Jig, which contains the entire peptide sequence of gp82, a metacyclic stage-specific surface glycoprotein implicated in target cell invasion. These data suggest ttl;it. in metacyclic trypomastigotes, gp82 is the signaling receptor that mediates protein tyrosine phosphorylation necessary for host cell invasion. (C) 1998 Academic Press.
Assunto Trypanosoma cruzi
metacyclic trypomastigotes
protein tyrosine phosphorylation
cell invasion
Idioma Inglês
Data 1998-06-01
Publicado em Experimental Parasitology. San Diego: Academic Press Inc, v. 89, n. 2, p. 188-194, 1998.
ISSN 0014-4894 (Sherpa/Romeo, fator de impacto)
Editor Academic Press Inc
Extensão 188-194
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000074135600006

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