Myosin A tail domain interacting protein (MTIP) localizes to the inner membrane complex of Plasmodium sporozoites

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Updated: Sep 28, 2026

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
08:07

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry

Published on: July 26, 2019

Lawrence W Bergman1, Karine Kaiser, Hisashi Fujioka

  • 1Division of Molecular Parasitology, Department of Microbiology & Immunology, Drexel University College of Medicine, Philadelphia, PA 19129, USA. lawrence.bergman@drexel.edu

Journal of Cell Science
|November 29, 2002
PubMed

Insights

Researchers identified MTIP, a novel protein interacting with Myosin A (MyoA), crucial for apicomplexan host cell invasion and motility. This discovery refines models of the parasite

Area of Science:

  • Parasitology
  • Cell Biology
  • Molecular Motors

Background:

  • Apicomplexan host cell invasion and motility rely on the actomyosin system.
  • Myosin A (MyoA) is the key motor protein in this system.
  • The precise components and interactions within the apicomplexan actomyosin motor complex remain incompletely understood.

Purpose of the Study:

  • To identify novel proteins interacting with Myosin A (MyoA).
  • To elucidate the molecular mechanisms underlying apicomplexan motility and host cell invasion.
  • To refine existing models of the apicomplexan actomyosin motor complex.

Main Methods:

  • Yeast two-hybrid screening using MyoA neck and tail domains as bait.
  • Deletion analysis to map protein interaction domains.
  • Immunofluorescence localization studies in Plasmodium sporozoites.

Main Results:

  • MTIP, a novel 24 kDa protein, was identified as an interactor of MyoA.
  • The C-terminal 15 amino acids of MyoA's tail domain specifically bind MTIP.
  • MTIP and MyoA co-localize within the inner membrane complex (IMC) of Plasmodium sporozoites.

Conclusions:

  • MTIP interacts with MyoA's tail domain, potentially immobilizing the motor at the IMC.
  • This interaction is proposed to be essential for the MyoA-driven motility and host cell invasion mechanism.
  • The findings support a model where MyoA drives actin filament redistribution for parasite movement and invasion.

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