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Structural studies on a putative protective Plasmodium knowlesi merozoite antigen.

J A Deans1, W C Jean

  • 1Department of Immunology, UMDS, Guy's Hospital Medical School, London, U.K.

Molecular and Biochemical Parasitology
|November 1, 1987
PubMed
Summary

Two monoclonal antibodies target a Plasmodium knowlesi antigen crucial for merozoite invasion. This antigen

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Area of Science:

  • Parasitology
  • Immunology
  • Molecular Biology

Background:

  • Plasmodium knowlesi merozoites invade erythrocytes, a critical step in malaria pathogenesis.
  • Specific antigens on the merozoite surface are targets for host immunity and intervention.

Purpose of the Study:

  • To characterize a Plasmodium knowlesi antigen recognized by inhibitory monoclonal antibodies.
  • To investigate the structure and properties of the epitope involved in merozoite invasion.

Main Methods:

  • Monoclonal antibody characterization
  • Antigen processing analysis
  • Epitope stability assessment
  • Antiserum inhibition assays

Main Results:

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  • Two monoclonal antibodies bind to a 66 kDa Plasmodium knowlesi antigen, preventing merozoite invasion.
  • The antigen is processed into 44 and 42 kDa fragments expressed on the merozoite surface.
  • The epitope is conformation-dependent, labile, and destroyed by SDS treatment.
  • Antiserum against native antigen inhibited parasite proliferation, while antiserum against SDS-treated antigen did not.

    • Conclusions:

    • The monoclonal antibody-defined epitope on the Plasmodium knowlesi antigen is essential for merozoite invasion.
    • The conformational integrity of this epitope is critical for its function and immunogenicity.