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What are Viruses?00:50

What are Viruses?

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Overview
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Membrane Fluidity01:23

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Cell membranes are composed of phospholipids, proteins, and carbohydrates loosely attached to one another through chemical interactions. Molecules are generally able to move about in the plane of the membrane, giving the membrane its flexible nature called fluidity. Two other features of the membrane contribute to membrane fluidity: the chemical structure of the phospholipids and the presence of cholesterol in the membrane.
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Membrane Fluidity01:26

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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...
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Intracellular bacteria and viruses often comprise a group of highly infectious pathogens that can cause several diseases. Bacterial pathogens include those belonging to the genus Rickettsia responsible for conditions such as rocky mountain spotted fever and the Mediterranean spotted fever; Chlamydia, a genus responsible for a sexually transmitted disease; Coxiella burnetii, an agent responsible for Q fever. Viral pathogens include vaccinia—a poxvirus, and herpes simplex virus—a...
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Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
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Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
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Simple and Robust in vivo and in vitro Approach for Studying Virus Assembly
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Virus entry, assembly, budding, and membrane rafts.

Nathalie Chazal1, Denis Gerlier

  • 1Immunologie-Virologie, EA 3038, Université Paul Sabatier, 31062 Toulouse, France. chazal@cict.fr

Microbiology and Molecular Biology Reviews : MMBR
|June 10, 2003
PubMed
Summary

Viruses utilize cellular machinery, including specialized membrane rafts, for replication. These lipid-rich microdomains facilitate viral entry, assembly, and budding, enhancing infection efficiency.

Area of Science:

  • Cell Biology
  • Virology
  • Biochemistry

Background:

  • Viruses are intracellular parasites dependent on host cell machinery.
  • Cell membranes exhibit heterogeneous lipid distribution, forming specialized microdomains.
  • Membrane rafts, enriched in sphingolipids and cholesterol, are involved in cellular processes like transport and signaling.

Purpose of the Study:

  • To review evidence supporting the role of membrane rafts in viral replication.
  • To propose models illustrating how viruses exploit membrane rafts.
  • To highlight the significance of lipid microdomains in viral infection.

Main Methods:

  • Literature review of existing studies on membrane rafts and viral replication.
  • Analysis of data implicating rafts in viral entry, assembly, and budding.

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  • Development of theoretical models for raft-virus interactions.

    • Main Results:

    • Evidence suggests viruses leverage membrane rafts for critical replication steps.
    • Rafts act as platforms for viral assembly and budding.
    • Specific protein-protein interactions crucial for infection are enhanced within rafts.

    Conclusions:

    • Membrane rafts provide a unique environment that promotes viral replication.
    • While direct proof is often lacking, rafts are strongly implicated in viral life cycles.
    • Targeting raft functions could offer new antiviral strategies.