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Trypanosoma cruzi GP63 proteins undergo stage-specific differential posttranslational modification and are important

Manjusha M Kulkarni1, Cheryl L Olson, David M Engman

  • 1Division of Infectious Diseases and Center for Microbial Interface Biology, The Ohio State University, Biomedical Research Tower, Rm. 1012, 460 W. 12th Ave., Columbus, OH 43210-1240, USA.

Infection and Immunity
|March 11, 2009
PubMed

Insights

Trypanosoma cruzi metalloprotease GP63 (TcGP63) has different forms and locations across its life cycle. Specific TcGP63 isoforms are crucial for host cell infection by the parasite.

Area of Science:

  • Parasitology
  • Molecular Biology
  • Biochemistry

Background:

  • Trypanosoma cruzi causes Chagas disease.
  • GP63 metalloproteases are important virulence factors in trypanosomatids.
  • Understanding TcGP63 function is key to developing interventions.

Purpose of the Study:

  • To investigate the expression, localization, and function of Trypanosoma cruzi GP63 (TcGP63) isoforms.
  • To determine the role of TcGP63 in host cell infection.

Main Methods:

  • Western blot analysis using specific antisera.
  • Surface biotinylation and endoglycosidase digestion.
  • Immunofluorescence microscopy.
  • Inhibition assays with antisera and protein fragments.

Main Results:

  • TcGP63 exists as distinct 61 kDa and 55 kDa isoforms, with stage-specific expression.
  • TcGP63 is an ecto-glycoprotein in epimastigotes and intracellular in metacyclic trypomastigotes.
  • TcGP63 isoforms are not raft-associated in T. cruzi.
  • TcGP63 plays a role in host cell infection, as blocking it reduces myoblast invasion.

Conclusions:

  • TcGP63 is expressed throughout the T. cruzi life cycle with stage-specific variations.
  • Different TcGP63 isoforms contribute to the parasite's ability to infect host cells.
  • TcGP63 represents a potential target for anti-Chagas disease therapies.

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