Related Experiment Video

Updated: Apr 27, 2026

Visualization of HIV-1 Gag Binding to Giant Unilamellar Vesicle GUV Membranes
08:21

Visualization of HIV-1 Gag Binding to Giant Unilamellar Vesicle GUV Membranes

Published on: July 28, 2016

8.2K

Roles played by acidic lipids in HIV-1 Gag membrane binding

Balaji Olety1, Akira Ono1

  • 1Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI 48109, United States.

Virus Research
|July 8, 2014
PubMed

Insights

HIV-1 Gag protein targets the plasma membrane for virus assembly, a process facilitated by interactions with acidic phospholipids like PI(4,5)P2. RNA binding can hinder this interaction, but PI(4,5)P2 helps overcome this block.

Area of Science:

  • Virology
  • Molecular Biology
  • Biochemistry

Background:

  • The MA domain of HIV-1 Gag is crucial for targeting the virus to the plasma membrane (PM).
  • Gag binding to lipid membranes is promoted by interactions with acidic phospholipids and its N-terminal myristoyl group.
  • Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), a PM-specific phosphoinositide, is vital for HIV-1 Gag localization and virus production.

Purpose of the Study:

  • To review the current understanding of HIV-1 Gag-membrane interactions.
  • To discuss the role of acidic phospholipids in HIV-1 assembly and Gag targeting.

Main Methods:

  • Literature review of studies on HIV-1 Gag-membrane interactions.
  • Analysis of the molecular mechanisms governing Gag localization and lipid binding.

Main Results:

  • MA domain-mediated targeting and assembly of HIV-1 Gag at the PM.
  • Acidic phospholipids, particularly PI(4,5)P2, are essential for Gag membrane association.
  • MA-bound RNA negatively regulates Gag-membrane binding, with PI(4,5)P2 overcoming this inhibition.

Conclusions:

  • Acidic phospholipids play a critical role in regulating HIV-1 Gag's interaction with the plasma membrane.
  • Understanding these interactions is key to understanding HIV-1 assembly and developing antiviral strategies.
Keywords:
Acyl chainsHIV-1 GagMembrane bindingPI(4,5)P(2)Virus assembly

More Related Videos

Author Spotlight: Advancing Cell Membrane Biophysics - Exploring Interactions and Challenges Through Experimental and Computational Approaches07:31

Author Spotlight: Advancing Cell Membrane Biophysics - Exploring Interactions and Challenges Through Experimental and Computational Approaches

Published on: September 1, 2023

3.3K
Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay07:10

Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay

Published on: September 14, 2014

13.8K

Related Concept Videos

Rab Proteins01:14

Rab Proteins

Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
4.0K
Lipids as Anchors01:32

Lipids as Anchors

In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains...
6.0K
Amino acids03:42

Amino acids

Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible...
72.8K
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
3.5K
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...
6.2K
Membrane Lipids01:32

Membrane Lipids

Lipids are an essential component of all biological membranes. The average lipid content in mammalian membranes is 50%, though it can be as low as 20% in the inner mitochondrial membrane or as high as 80% in the myelin sheath present around the nerve cells.
Phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, and sphingomyelin are the most common phospholipids present in mammalian membranes. At physiological pH, phosphatidylserine is negatively charged, while the other three...
19.5K