Related Experiment Video

Updated: Feb 21, 2026

Preparing Lamellae from Vitreous Biological Samples Using a Dual-Beam Scanning Electron Microscope for Cryo-Electron Tomography
07:00

Preparing Lamellae from Vitreous Biological Samples Using a Dual-Beam Scanning Electron Microscope for Cryo-Electron Tomography

Published on: August 5, 2021

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Proteome and Structural Organization of the Knob Complex on the Surface of the Plasmodium Infected Red Blood Cell

Shuba Varshini Alampalli1, Manish Grover1, Syama Chandran1

  • 1Department of Biochemistry, Indian Institute of Science, Bangalore, India.

Proteomics. Clinical Applications
|October 6, 2017
PubMed
Abstract

Insights

Researchers identified new proteins in malaria parasite knobs, crucial for virulence. This structural insight aids in developing new malaria vaccines and drugs targeting knob destabilization.

Area of Science:

  • Malariology
  • Structural Biology
  • Proteomics

Background:

  • The malaria parasite Plasmodium falciparum forms 'knobs' on infected erythrocyte membranes.
  • Knob structure, particularly PfEMP1, determines cytoadhesion, rosetting, and immune evasion.

Purpose of the Study:

  • To comprehensively identify the knob proteome.
  • To gain structural insights into knob component organization.

Main Methods:

  • Proteomics analysis of detergent-resistant membrane rafts from infected erythrocytes.
  • Ab initio structural modeling of knob components.

Main Results:

  • Identified novel knob components including host Hsp70, elongation factor 1A, and acyl CoA synthetase.
  • Structural predictions reveal intrinsically disordered proteins with variable interaction capabilities.
  • PfEMP1-PHIST repeat units are numerous on the knob periphery.

Conclusions:

  • Provides structural insights into knob organization and identifies novel components.
  • Structural information can inform vaccine and drug design against P. falciparum malaria virulence factors.
Keywords:
Plasmodium falciparumcytoadhesionknobsmalariamodeling

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