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Heterologous Expression of A Trypanosoma Cruzi Surface Glycoprotein (Gp82) In Mammalian Cells Indicates the Existence of Different Signal Sequence Requirements and Processing
Author(s) -
RAMIREZ MARCEL I.,
BOSCARDIN SILVIA B.,
HAN SANG W.,
PARANHOSBACCALA GLAUCIA,
YOSHIDA NOBUKO,
KELLY JOHN M.,
MORTARA RENATO A.,
SILVEIRA JOSÉ FRANCO DA
Publication year - 1999
Publication title -
journal of eukaryotic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 1066-5234
DOI - 10.1111/j.1550-7408.1999.tb05131.x
Subject(s) - biology , trypanosoma cruzi , glycoprotein , signal peptide , endoplasmic reticulum , transfection , microbiology and biotechnology , cell sorting , membrane glycoproteins , gene , heterologous , peptide sequence , parasite hosting , cell , biochemistry , world wide web , computer science
Metacyclic trypomastigotes of Trypanosoma cruzi express a developmentally regulated 82 kDa surface glycoprotein (gp82) that has been implicated in the mammalian cell invasion. When the non‐infective epimastigote stage of the parasite was transfected with a vector containing the gp82 gene, an 82 kDa surface glycoprotein, which was indistinguishable from the metacyclic stage protein, was expressed. In contrast, when the same gene was expressed in transfected mammalian cells, although a large amount of protein was produced, it was not imported into the endoplasmic reticulum and glycosylated. This blockage in targeting and processing could be partially compensated for by the addition of a virus haemagglutinin signal peptide to the amino terminus of gp82. Thus, the requirements for membrane protein processing are distinct in mammals and T. cruzi , and an intrinsic feature of the gp82 prevents subsequent sorting to the mammalian cell surface. These results could be useful in the development of new DNA vaccines against T. cruzi employing parasite genes encoding immunodominant surface glycoproteins.