Document Detail


The interplay between folding-facilitating mechanisms in Trypanosoma cruzi endoplasmic reticulum.
MedLine Citation:
PMID:  12972544     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Lectin (calreticulin [CRT])-N-glycan-mediated quality control of glycoprotein folding is operative in trypanosomatid protozoa but protein-linked monoglucosylated N-glycans are exclusively formed in these microorganisms by UDP-Glc:glycoprotein glucosyltransferase (GT)-dependent glucosylation. The gene coding for this enzyme in the human pathogen Trypanosoma cruzi was identified and sequenced. Even though several of this parasite glycoproteins have been identified as essential components of differentiation and mammalian cell invasion processes, disruption of both GT-encoding alleles did not affect cell growth rate of epimastigote form parasites and only partially affected differentiation and mammalian cell invasion. The cellular content of one of the already identified T. cruzi glycoprotein virulence factors (cruzipain, a lysosomal proteinase) only showed a partial (5-20%) decrease in GT null mutants in spite of the fact that >90% of all cruzipain molecules interacted with CRT during their folding process in wild-type cells. Although extremely mild cell lysis and immunoprecipitation procedures were used, no CRT-cruzipain interaction was detected in GT null mutants but secretion of the proteinase was nevertheless delayed because of a lengthened interaction with Grp78/BiP probably caused by the detected induction of this chaperone in GT null mutants. This result provides a rationale for the absence of a more drastic consequence of GT absence. It was concluded that T. cruzi endoplasmic reticulum folding machinery presents an exquisite plasticity that allows the parasite to surmount the absence of the glycoprotein-specific folding facilitation mechanism.
Authors:
Ianina Conte; Carlos Labriola; Juan J Cazzulo; Roberto Docampo; Armando J Parodi
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.     Date:  2003-06-27
Journal Detail:
Title:  Molecular biology of the cell     Volume:  14     ISSN:  1059-1524     ISO Abbreviation:  Mol. Biol. Cell     Publication Date:  2003 Sep 
Date Detail:
Created Date:  2003-09-15     Completed Date:  2004-04-08     Revised Date:  2013-06-09    
Medline Journal Info:
Nlm Unique ID:  9201390     Medline TA:  Mol Biol Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3529-40     Citation Subset:  IM    
Affiliation:
Institute for Biotechnological Research, University of San Martin, CC30, (1650) San Martin, Argentina.
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MeSH Terms
Descriptor/Qualifier:
Animals
Base Sequence
Calreticulin / metabolism
Cell Differentiation / physiology
Cell Survival / physiology
Cells, Cultured
Cloning, Molecular
Cysteine Endopeptidases / metabolism*
Endoplasmic Reticulum / enzymology*
Glucosyltransferases / metabolism*,  secretion
Heat-Shock Proteins / metabolism*
Molecular Sequence Data
Myoblasts / physiology
Protein Folding
Protein Processing, Post-Translational
Protozoan Proteins / metabolism*
Sequence Analysis
Trypanosoma cruzi / enzymology*
Chemical
Reg. No./Substance:
0/Calreticulin; 0/Heat-Shock Proteins; 0/Protozoan Proteins; EC 2.4.1.-/Glucosyltransferases; EC 2.4.1.-/mannosylglycoprotein 1,3-glucosyltransferase; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.4.22.-/cruzipain
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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