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The closed MTIP-myosin A-tail complex from the malaria parasite invasion machinery

Jürgen Bosch1, Stewart Turley, Claudia M Roach

  • 1Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.

Journal of Molecular Biology
|July 14, 2007
PubMed

Insights

The malaria parasite's Myosin A-tail interacting protein (MTIP) forms a compact complex with Myosin A at neutral pH. This structure is crucial for host cell invasion and offers potential for new antimalarial drug development.

Area of Science:

  • Structural biology
  • Parasitology
  • Biochemistry

Background:

  • Myosin A-tail interacting protein (MTIP) is essential for malaria parasite invasion.
  • MTIP links the actomyosin motor to the inner membrane complex during host cell invasion.

Purpose of the Study:

  • To elucidate the structural basis of the MTIP:Myosin A complex formation.
  • To identify key residues involved in the MTIP:Myosin A interaction.
  • To explore potential therapeutic targets for malaria parasite invasion inhibitors.

Main Methods:

  • X-ray crystallography to determine the structure of the MTIP:Myosin A complex.
  • Site-directed mutagenesis to investigate the role of specific amino acid residues.
  • Biochemical assays to assess complex formation and function.

Main Results:

  • At neutral pH, Plasmodium falciparum MTIP and Myosin A form a compact complex, unlike previously observed extended structures.
  • Myosin A residues H810 and K813 are critical for the compact complex formation.
  • The unprotonated state of Myosin A-H810 and extensive interactions with Myosin A-K813 are essential for this compact conformation.

Conclusions:

  • The compact MTIP:Myosin A structure reveals a novel conformation important for parasite invasion.
  • Key residues H810 and K813 of Myosin A play essential roles in stabilizing this compact complex.
  • The adaptable nature of MTIP structures suggests potential for developing inhibitors targeting malaria parasite cell invasion.

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