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|Title:||Characterization of a 21 kDa protein from Trypanosoma cruzi associated with mammalian cell invasion|
|Authors:||Silva, Claudio V. da [UNIFESP]|
Kawashita, Silvia Y. [UNIFESP]
Probst, Christian M.
Cruz, Mario C. [UNIFESP]
Silva, Erika A. da [UNIFESP]
Souto-Padron, Thais C. B. S.
Krieger, Marco A.
Briones, Marcelo R. S. [UNIFESP]
Andrews, Norma W.
Mortara, Renato A. [UNIFESP]
Universidade Federal de São Paulo (UNIFESP)
Universidade Federal do Rio de Janeiro (UFRJ)
|Citation:||Microbes and Infection. Amsterdam: Elsevier B.V., v. 11, n. 5, p. 563-570, 2009.|
|Abstract:||Trypanosoma cruzi genomic database was screened for hypothetical proteins that showed high probability of being secreted or membrane anchored and thus, likely involved in host-cell invasion. A sequence that codes for a 21 kDa protein that showed high probability of being secreted was selected. After cloning this protein sequence, the results showed that it was a ubiquitous protein and secreted by extracellular amastigotes. the recombinant form (P21-His(6)) adhered to HeLa cells in a dose-dependent manner. Pretreatment of host cells with P21-His(6) inhibited cell invasion by extracellular amastigotes from G and CL strains. On the other hand, when the protein was added to host cells at the same time as amastigotes, an increase in cell invasion was observed. Host-cell pretreatment with P21-His(6) augmented invasion by metacyclic trypomastigotes. Moreover, polyclonal antibody anti-P21 inhibited invasion only by extracellular amastigotes and metacyclic trypomastigotes from G strain. These results suggested that P21 might be involved in T. cruzi cell invasion. We hypothesize that P21 could be secreted in the juxtaposition parasite-host cell and triggers signaling events yet unknown that lead to parasite internalization. (C) 2009 Elsevier Masson SAS. All rights reserved.|
|Appears in Collections:||Em verificação - Geral|
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