Trypanosoma cruzi glycoprotein 72: Immunological analysis and cellular localization

1992 ◽  
Vol 109 (1) ◽  
pp. 25-36 ◽  
Author(s):  
Guenter Harth ◽  
Alea A. Mills ◽  
Thais Souto-Padrón ◽  
Wanderley de Souza
Keyword(s):  
Trypanosoma Cruzi ◽  
Cellular Localization ◽  
Immunological Analysis

scholarly journals Trypanosoma cruzi Presenilin-Like Transmembrane Aspartyl Protease: Characterization and Cellular Localization

Biomolecules ◽  
2020 ◽  
Vol 10 (11) ◽  
pp. 1564
Author(s):  
Guilherme C. Lechuga ◽  
Paloma Napoleão-Pêgo ◽  
Carolina C. G. Bottino ◽  
Rosa T. Pinho ◽  
David W. Provance-Jr ◽  
...  
Keyword(s):  
Trypanosoma Cruzi ◽  
Cellular Localization ◽  
Secretory Pathway ◽  
Chronic Phase ◽  
Basic Research ◽  
New Drugs ◽  
Public Health Issue ◽  
Spot Synthesis ◽  
Major Public Health Issue ◽  
Computational Analyses

The increasing detection of infections of Trypanosoma cruzi, the etiological agent of Chagas disease, in non-endemic regions beyond Latin America has risen to be a major public health issue. With an impact in the millions of people, current treatments rely on antiquated drugs that produce severe side effects and are considered nearly ineffective for the chronic phase. The minimal progress in the development of new drugs highlights the need for advances in basic research on crucial biochemical pathways in T. cruzi to identify new targets. Here, we report on the T. cruzi presenilin-like transmembrane aspartyl enzyme, a protease of the aspartic class in a unique phylogenetic subgroup with T. vivax separate from protozoans. Computational analyses suggest it contains nine transmembrane domains and an active site with the characteristic PALP motif of the A22 family. Multiple linear B-cell epitopes were identified by SPOT-synthesis analysis with Chagasic patient sera. Two were chosen to generate rabbit antisera, whose signal was primarily localized to the flagellar pocket, intracellular vesicles, and endoplasmic reticulum in parasites by whole-cell immunofluorescence. The results suggest that the parasitic presenilin-like enzyme could have a role in the secretory pathway and serve as a target for the generation of new therapeutics specific to the T. cruzi.

scholarly journals Expression and Cellular Localization of Molecules of the gp82 Family in Trypanosoma cruzi Metacyclic Trypomastigotes

2007 ◽  
Vol 75 (7) ◽  
pp. 3264-3270 ◽  
Author(s):  
Vanessa D. Atayde ◽  
Mauro Cortez ◽  
Renata Souza ◽  
José Franco da Silveira ◽  
Nobuko Yoshida
Keyword(s):  
Trypanosoma Cruzi ◽  
Host Cell ◽  
Cell Invasion ◽  
Cellular Localization ◽  
Polyclonal Antibodies ◽  
Microscopic Analysis ◽  
Cdna Clones ◽  
Host Cell Invasion ◽  
Two Dimensional Gel Electrophoresis ◽  
Surface Localization

ABSTRACT A member of the Trypanosoma cruzi gp82 family, expressed on metacyclic trypomastigote surface and identified by monoclonal antibody (MAb) 3F6, plays a key role in host cell invasion. Apart from the gp82 defined by MAb 3F6, no information is available on members of this protein family. From cDNA clones encoding gp82 proteins sharing 59.1% sequence identity, we produced the recombinant proteins J18 and C03, the former containing and the latter lacking the epitope for MAb 3F6. Polyclonal antibodies to J18 and C03 proteins were generated and used, along with MAb 3F6, to analyze the expression and cellular localization of gp82 family members in metacyclic forms of CL and G strains, which belong to highly divergent genetic groups. By two-dimensional gel electrophoresis and immunoblotting, molecules of 82 to 86 kDa, focusing at pH 4.6 to 5.4, and molecules of 72 to 88 kDa, focusing at pH 4.9 to 5.7, were visualized in CL and G strains, respectively. Flow cytometry and microscopic analysis revealed in both strains similar expression of MAb 3F6-reactive gp82 in live and permeabilized parasites, indicating its surface localization. The reaction of live parasites of both strains with anti-J18 antibodies was weaker than with MAb 3F6 and was increased by permeabilization. Anti-C03 antibodies bound predominantly to flagellar components in permeabilized G strain parasites, but in the CL strain the flagellum was not the preferential target for these antibodies. Host cell invasion of metacyclic forms was inhibited by J18 protein, as well as by MAb 3F6 and anti-J18 antibodies, but not by C03 protein or anti-C03 antibodies.

Expression and cellular localization of Trypanosoma cruzi type II DNA topoisomerase

1998 ◽  
Vol 94 (2) ◽  
pp. 197-204 ◽  
Author(s):  
Stenio P Fragoso ◽  
Denise Mattei ◽  
Jane C Hines ◽  
Dan Ray ◽  
Samuel Goldenberg
Keyword(s):  
Trypanosoma Cruzi ◽  
Cellular Localization ◽  
Type Ii ◽  
Dna Topoisomerase

TcRho1 of Trypanosoma cruzi: role in metacyclogenesis and cellular localization

2004 ◽  
Vol 323 (3) ◽  
pp. 1009-1016 ◽  
Author(s):  
Luiz Dione B. de Melo ◽  
José L. Nepomuceno-Silva ◽  
Celso Sant’Anna ◽  
Nicole Eisele ◽  
Rodrigo B. Ferraro ◽  
...  
Keyword(s):  
Trypanosoma Cruzi ◽  
Cellular Localization

scholarly journals Trypanosoma Cruzi Presenilin-like Transmembrane Aspartyl Protease: Characterization and Cellular Localization

2020 ◽  
Author(s):  
Guilherme C. Lechuga ◽  
Paloma Napoleão-Pêgo ◽  
Carolina C.G. Bottino ◽  
Rosa T. Pinho ◽  
David W. Provance-Jr ◽  
...  
Keyword(s):  
Trypanosoma Cruzi ◽  
Cellular Localization ◽  
Secretory Pathway ◽  
Chronic Phase ◽  
Basic Research ◽  
New Drugs ◽  
Public Health Issue ◽  
Spot Synthesis ◽  
Major Public Health Issue ◽  
Computational Analyses

The increasing detection of infections of Trypanosoma cruzi, the etiological agent of Chagas disease, in non-endemic regions beyond Latin America has risen to be a major public health issue. With an impact in the millions of people, current treatments rely on antiquated drugs that produce severe side effects and are considered nearly ineffective for the chronic phase. The minimal progress in the development of new drugs highlights the need for advances in basic research on crucial biochemical pathways in T. cruzi to identify new targets. Here, we report on the T. cruzi presenilin-like transmembrane aspartyl enzyme, a protease of the aspartic class in a unique phylogenetic subgroup with T. vivax separate from protozoans. Computational analyses suggests it contains 9 transmembrane domains and an active site with the characteristic PALP motif of the A22 family. Multiple linear B-cell epitopes were identified by SPOT synthesis analysis with Chagasic patient sera. Two were chosen to generate rabbit antisera, whose signal was primarily localized to the flagellar pocket, intracellular vesicles and endoplasmic reticulum in parasites by whole cell immunofluorescence. The results suggest that the parasitic presenilin-like enzyme could have a role in the secretory pathway and serve as a biomarker for infections.

Isolation and immunological analysis of Trypanosoma cruzi glycolipids

Acta Tropica ◽  
1991 ◽  
Vol 48 (3) ◽  
pp. 233-241 ◽  
Author(s):  
S.Giovanni De Simone ◽  
R.T. Pinho ◽  
C.M.M. Vanni ◽  
L.C.Pontes de Carvalho
Keyword(s):  
Trypanosoma Cruzi ◽  
Immunological Analysis

scholarly journals Distinct genomic organization, mRNA expression and cellular localization of members of two amastin sub-families present in Trypanosoma cruzi

2013 ◽  
Vol 13 (1) ◽  
pp. 10 ◽  
Author(s):  
Monica Mendes Kangussu-Marcolino ◽  
Rita Márcia Cardoso de Paiva ◽  
Patrícia Rosa Araújo ◽  
Rondon Pessoa de Mendonça-Neto ◽  
Laiane Lemos ◽  
...  
Keyword(s):  
Trypanosoma Cruzi ◽  
Mrna Expression ◽  
Cellular Localization ◽  
Genomic Organization

The Immuno-Electron Microscopic Localization of the Mo-Fe Protein Component of Nitrogenase in Cells of Azotobacter Vinelandii

1973 ◽  
Vol 31 ◽  
pp. 574-575
Author(s):  
J. T. Stasny ◽  
R. C. Burns ◽  
R. W. F. Hardy
Keyword(s):  
Cellular Localization ◽  
Direct Evidence ◽  
Azotobacter Vinelandii ◽  
Intracellular Localization ◽  
Protein Component ◽  
Electron Microscopic ◽  
Thin Sections ◽  
Fe Protein ◽  
Intracytoplasmic Membranes

Structure-functlon studies of biological N2-fixation have correlated the presence of the enzyme nitrogenase with increased numbers of intracytoplasmic membranes in Azotobacter. However no direct evidence has been provided for the internal cellular localization of any nitrogenase. Recent advances concerned with the crystallizatiorTand the electron microscopic characterization of the Mo-Fe protein component of Azotobacter nitrogenase, prompted the use of this purified protein to obtain antibodies (Ab) to be conjugated to electron dense markers for the intracellular localization of the protein by electron microscopy. The present study describes the use of ferritin conjugated to goat antitMo-Fe protein immunoglobulin (IgG) and the observations following its topical application to thin sections of N2-grown Azotobacter.

Mucin gene expression in OME: cellular localization

1998 ◽  
Vol 23 (3) ◽  
pp. 281-282
Author(s):  
Hutton ◽  
Guo ◽  
Birchall ◽  
Pearson
Keyword(s):  
Gene Expression ◽  
Cellular Localization ◽  
Mucin Gene

Protective effect of Trypanosoma rangeli against infections with a highly virulent strain of Trypanosoma cruzi

1997 ◽  
Vol 2 (5) ◽  
pp. 482-487 ◽  
Author(s):  
Claudio Zuniga ◽  
Teresa Palau ◽  
Pilar Penin ◽  
Carlos Gamallo ◽  
Jose Antonio de Diego
Keyword(s):  
Trypanosoma Cruzi ◽  
Protective Effect ◽  
Virulent Strain ◽  
Trypanosoma Rangeli ◽  
Highly Virulent
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