Related Experiment Video

Updated: Feb 14, 2026

Separation of Plasmodium falciparum Late Stage-infected Erythrocytes by Magnetic Means
05:20

Separation of Plasmodium falciparum Late Stage-infected Erythrocytes by Magnetic Means

Published on: March 2, 2013

14.4K

In silico guided reconstruction and analysis of ICAM-1-binding var genes from Plasmodium falciparum

Eilidh Carrington1,2, Thomas D Otto3,4, Tadge Szestak1

  • 1Liverpool School of Tropical Medicine, Pembroke Place, Liverpool, L3 5QA, UK.

Scientific Reports
|February 21, 2018
PubMed

Insights

Researchers reconstructed full-length var genes, which encode Plasmodium falciparum variant surface antigen 1 (PfEMP1), from sequence tags of infected erythrocytes. This advance enables further biophysical analysis of PfEMP1 domains involved in severe malaria pathology.

Area of Science:

  • Malariology
  • Molecular Biology
  • Genomics

Background:

  • Plasmodium falciparum variant surface antigen 1 (PfEMP1) on infected erythrocytes is crucial for severe malaria pathology.
  • The var gene family encoding PfEMP1 is highly diverse, complicating full-length gene reconstruction.
  • Reconstructing full-length var genes from sequence tags offers a pathway to study PfEMP1 function.

Purpose of the Study:

  • To determine if full-length var genes can be reconstructed from small sequence tags.
  • To identify the full-length PfEMP1 expressed by laboratory-adapted parasite isolates.
  • To enable biophysical analyses of PfEMP1 ICAM-1 binding regions.

Main Methods:

  • Generation of sequence tags from laboratory-adapted ICAM-1-binding Plasmodium falciparum isolates.
  • Bioinformatic reconstruction of full-length var genes from sequence tags.
  • Validation of reconstructed var gene sequences.
  • Biophysical analysis of ICAM-1 binding regions of expressed PfEMP1.

Main Results:

  • Successful reconstruction of validated, full-length var gene sequences from sequence tags in a subset of isolates.
  • Identification of the full-length PfEMP1 expressed by these parasite isolates.
  • Enabled biophysical characterization of PfEMP1 ICAM-1 binding domains.

Conclusions:

  • Reconstructing full-length var genes from sequence tags is feasible.
  • This method facilitates the study of PfEMP1 diversity and function in severe malaria.
  • Further biophysical analyses of PfEMP1 domains are now possible.

More Related Videos

Methods to Investigate the Regulatory Role of Small RNAs and Ribosomal Occupancy of Plasmodium falciparum10:22

Methods to Investigate the Regulatory Role of Small RNAs and Ribosomal Occupancy of Plasmodium falciparum

Published on: December 4, 2015

9.4K
Selection of Plasmodium falciparum Parasites for Cytoadhesion to Human Brain Endothelial Cells10:09

Selection of Plasmodium falciparum Parasites for Cytoadhesion to Human Brain Endothelial Cells

Published on: January 3, 2012

19.5K

Related Concept Videos

The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
15.2K
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

10.1K
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form...
7.4K
Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
15.2K
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
5.2K
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
5.6K