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Onchocerca retinol- and ivermectin-binding protein activity

P G Lal1, E R James

  • 1Department of Ophthalmology, Medical University of South Carolina, Charleston 29425, USA.

Parasitology
|February 1, 1996
PubMed
Summary

Researchers identified a specific retinol-binding protein (RBP) in Onchocerca worms, approximately 19.7 kDa. Ivermectin interferes with retinol binding to this protein, suggesting a potential mechanism for its antiparasitic effects.

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Area of Science:

  • Parasitology
  • Biochemistry
  • Molecular Biology

Background:

  • Onchocerca cervicalis is a nematode parasite causing onchocerciasis.
  • Retinol-binding proteins (RBPs) are crucial for vitamin A transport and metabolism.
  • Ivermectin is a key drug for treating onchocerciasis, but its precise molecular targets are not fully elucidated.

Purpose of the Study:

  • To investigate the presence and characteristics of retinol-binding protein (RBP) activity in Onchocerca cervicalis adult worms.
  • To examine the interaction between retinol binding and ivermectin in these parasites.
  • To identify potential molecular targets of ivermectin.

Main Methods:

  • High-pressure size exclusion chromatography (HPSEC) was used to analyze [3H]-retinol and [3H]-ivermectin binding.

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  • Competition assays with non-labeled retinol and ivermectin were performed to determine binding specificity.

    • Main Results:

    • Four distinct molecular weight fractions (150, 67, 19.7, and 4.6 kDa) showed [3H]-retinol incorporation.
    • Specific retinol binding was observed primarily at the 19.7 kDa fraction.
    • Ivermectin competed with retinol binding to the 19.7 kDa fraction.
    • Ivermectin binding showed a different molecular weight distribution compared to retinol, with a prominent 150 kDa fraction.
    • Both ivermectin and retinol inhibited [3H]-ivermectin binding to all detected fractions.

    Conclusions:

    • A putative Onchocerca RBP with an approximate molecular weight of 19.7 kDa was identified.
    • Retinol also binds non-specifically to other worm fractions.
    • Ivermectin binding differs quantitatively and qualitatively from retinol binding.
    • Ivermectin interferes with retinol binding to the specific 19.7 kDa Onchocerca protein, suggesting a potential mechanism of action.