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Related Concept Videos

Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
Membrane Domains01:18

Membrane Domains

The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
Membrane Fluidity01:26

Membrane Fluidity

Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
Mosaic nature of the membrane
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is a relatively...
Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that include the...
Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that include the...

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Related Experiment Video

Updated: May 20, 2026

Reconstitution of a Kv Channel into Lipid Membranes for Structural and Functional Studies
10:22

Reconstitution of a Kv Channel into Lipid Membranes for Structural and Functional Studies

Published on: July 13, 2013

Coronavirus E protein forms ion channels with functionally and structurally-involved membrane lipids.

Carmina Verdiá-Báguena1, Jose L Nieto-Torres, Antonio Alcaraz

  • 1Department of Physics, Laboratory of Molecular Biophysics, Universitat Jaume I, 12071 Castellón, Spain.

Virology
|July 27, 2012
PubMed
Summary

The severe acute respiratory syndrome coronavirus (SARS-CoV) envelope (E) protein forms an ion channel. This protein-lipid pore activity is influenced by the surrounding membrane lipids, suggesting a novel mechanism for coronavirus ion channel function.

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Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy
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Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy

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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

Related Experiment Videos

Last Updated: May 20, 2026

Reconstitution of a Kv Channel into Lipid Membranes for Structural and Functional Studies
10:22

Reconstitution of a Kv Channel into Lipid Membranes for Structural and Functional Studies

Published on: July 13, 2013

Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy
08:27

Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy

Published on: January 7, 2019

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

Area of Science:

  • Virology
  • Structural Biology
  • Biophysics

Background:

  • The coronavirus (CoV) envelope (E) protein is a key component of the viral structure.
  • The ion channel activity of the CoV E protein is implicated in viral pathogenesis.
  • Understanding the precise mechanism of E protein ion channel function is crucial for developing antiviral strategies.

Purpose of the Study:

  • To investigate the ion channel activity of the severe acute respiratory syndrome CoV (SARS-CoV) E protein.
  • To determine the role of transmembrane domain mutations in E protein ion channel function.
  • To elucidate the influence of lipid composition and charge on E protein ion channel activity.

Main Methods:

  • Reconstitution of SARS-CoV E protein and its transmembrane domain peptides into planar lipid bilayers.
  • Electrophysiological recordings to measure ion conductivity and selectivity.
  • Site-directed mutagenesis to assess the impact of specific amino acid changes (N15A, V25F) on ion channel function.

Main Results:

  • Both full-length SARS-CoV E protein and its transmembrane domain peptides formed voltage-independent ion conductive pores.
  • Mutations N15A and V25F within the transmembrane domain abolished ion conductivity.
  • E protein-derived channels exhibited altered cation selectivity based on lipid membrane charge, suggesting a protein-lipid pore formation.

Conclusions:

  • The SARS-CoV E protein functions as an ion channel, with its transmembrane domain being critical for pore formation.
  • Lipid composition and charge significantly modulate the ion channel activity and selectivity of the CoV E protein.
  • These findings propose a novel concept of a protein-lipid pore entity for coronavirus E protein ion channels.