ArticleInfection and immunity2003
gp63 homologues in Trypanosoma cruzi: surface antigens with metalloprotease activity and a possible role in host cell infection.
Article in Infection and immunity, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 123 citations in OpenAlex.
- Transcriptomic dynamics reveals sequential acquisition of complement resistance during prolonged starvation of Trypanosoma cruzi epimastigoteMemorias do Instituto Oswaldo Cruz · 2026Article
- Cardiac alterations induced by Trypanosoma cruzi extracellular vesicles and immune complexes.PLoS neglected tropical diseases · 2025Article
- Review
- Exploring the genomic landscape of the GP63 family in Trypanosoma cruzi: Evolutionary dynamics and functional peculiarities.PLoS neglected tropical diseases · 2025Article
- In silico evaluation of N-aryl-1,10-phenanthroline-2-amines as potential inhibitors of T. cruzi GP63 zinc-metalloprotease by docking and molecular dynamics simulations.Scientific reports · 2025Article
- Trypanosomatid Extracellular Vesicles as Potential Immunogens for Chagas Disease.International journal of molecular sciences · 2025Article
- Circulating extracellular vesicles in sera of chronic patients as a method for determining active parasitism in Chagas disease.PLoS neglected tropical diseases · 2024Article
- Interaction ofMicroorganisms · 2024Review
- Oral infectivity through carnivorism in murine model ofFrontiers in cellular and infection microbiology · 2024Article
- Genomes ofPathogens (Basel, Switzerland) · 2023Article
- Detection and activity of MMP-2 and MMP-9 in Leishmania amazonensis and Leishmania braziliensis promastigotes.BMC microbiology · 2023Article
- Review
- Metalloprotease Gp63-Targeting Novel Glycoside Exhibits Potential Antileishmanial Activity.Frontiers in cellular and infection microbiology · 2022Article
- Role of Virulence Factors of Trypanosomatids in the Insect Vector and Putative Genetic Events Involved in Surface Protein Diversity.Frontiers in cellular and infection microbiology · 2022Review
- Anti-Leishmania braziliensis activity of 1,10-phenanthroline-5,6-dione and its Cu(II) and Ag(I) complexes.Parasitology research · 2021Article
- Sialic acid removal by trans-sialidase modulates MMP-2 activity during Trypanosoma cruzi infection.Biochimie · 2021Article
- Biological and Molecular Effects ofFrontiers in cellular and infection microbiology · 2021Article
- The Glycosylphosphatidylinositol Anchor: A Linchpin for Cell Surface Versatility of Trypanosomatids.Frontiers in cell and developmental biology · 2021Review
- Slight temperature changes cause rapid transcriptomic responses in Trypanosoma cruzi metacyclic trypomastigotes.Parasites & vectors · 2020Article
- Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
gp63 is a highly abundant glycosylphosphatidylinositol (GPI)-anchored membrane protein expressed predominantly in the promastigote but also in the amastigote stage of Leishmania species. In Leishmania spp., gp63 has been implicated in a number of steps in establishment of infection. Here we demonstrate that Trypanosoma cruzi, the etiological agent of Chagas' disease, has a family of gp63 genes composed of multiple groups. Two of these groups, Tcgp63-I and -II, are present as high-copy-number genes. The genomic organization and mRNA expression pattern were specific for each group. Tcgp63-I was widely expressed, while the Tcgp63-II group was scarcely detected in Northern blots, even though it is well represented in the T. cruzi genome. Western blots using sera directed against a synthetic peptide indicated that the Tcgp63-I group produced proteins of approximately 78 kDa, differentially expressed during the life cycle. Immunofluorescence staining and phosphatidylinositol-specific phospholipase C digestion confirmed that Tcgp63-I group members are surface proteins bound to the membrane by a GPI anchor. We also demonstrate the presence of metalloprotease activity which is attributable, at least in part, to Tcgp63-I group. Since antibodies against Tcgp63-I partially blocked infection of Vero cells by trypomastigotes, a possible role for this group in infection is suggested.
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