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Involvement of Leishmania donovani major surface glycoprotein gp63 in promastigote multiplication

Sanjeev Pandey1, Phuljhuri Chakraborti, Rakhi Sharma

  • 1Indian Institute of Chemical Biology, Kolkata, India.

Journal of Biosciences
|August 3, 2004
PubMed

Insights

The Leishmania surface glycoprotein gp63 is crucial for parasite multiplication. Reducing gp63 levels in Leishmania donovani promastigotes impaired growth and altered cell cycle, suggesting a role beyond host cell interaction.

Area of Science:

  • Parasitology
  • Molecular Biology
  • Cell Biology

Background:

  • The Leishmania surface glycoprotein gp63 is a key virulence factor.
  • gp63 is believed to mediate parasite entry and survival within host macrophages.

Purpose of the Study:

  • To investigate the role of gp63 in Leishmania donovani promastigote multiplication.
  • To determine if gp63 has functions beyond host cell interactions.

Main Methods:

  • Leishmania donovani promastigotes were transfected with gp63 antisense RNA to create gp63-deficient cells.
  • Cell cycle progression, morphology, and growth rates were analyzed.
  • The effect of a recombinant gp63 fragment was assessed on cell growth and binucleation.

Main Results:

  • Reduced gp63 levels led to longer generation times and altered cell morphology.
  • gp63-deficient cells accumulated in the G2/M phase and showed increased binucleation.
  • A fusion protein containing gp63 domains stimulated growth and reduced binucleate cells.

Conclusions:

  • gp63 plays a significant role in promastigote multiplication, independent of its role in host cell invasion.
  • The fibronectin-like properties of gp63 may be critical for parasite proliferation.

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