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Related Concept Videos

Viral Structure00:56

Viral Structure

Viruses are extraordinarily diverse in shape and size, but they all have several structural features in common. All viruses have a core that contains a DNA- or RNA-based genome. The core is surrounded by a protective coat of proteins called the capsid. The capsid is composed of subunits called capsomeres. The capsid and genome-containing core are together known as the nucleocapsid.
Lytic Cycle of Bacteriophages01:30

Lytic Cycle of Bacteriophages

Bacteriophages, also known as phages, are specialized viruses that infect bacteria. A key characteristic of phages is their distinctive “head-tail” morphology. A phage begins the infection process (i.e., lytic cycle) by attaching to the outside of a bacterial cell. Attachment is accomplished via proteins in the phage tail that bind to specific receptor proteins on the outer surface of the bacterium. The tail injects the phage’s DNA genome into the bacterial cytoplasm. In the lytic replication...
Intracellular Movement of Viruses and Bacteria01:10

Intracellular Movement of Viruses and Bacteria

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 virus that...
Viral Replication: Lytic Cycle01:20

Viral Replication: Lytic Cycle

Bacteriophages, or phages, are viruses that specifically infect bacteria. Among them, T-even bacteriophages, such as T4, exhibit a well-characterized lytic replication cycle in Escherichia coli (E. coli). This process ensures the rapid proliferation of the virus while ultimately leading to the destruction of the bacterial host.Attachment and DNA InjectionThe infection process begins with the recognition and binding of the T4 phage to the E. coli cell surface. Tail fibers of the phage...
What are Viruses?00:50

What are Viruses?

Overview
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...

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Related Experiment Video

Updated: May 11, 2026

A Fluorogenic Peptide Cleavage Assay to Screen for Proteolytic Activity: Applications for coronavirus spike protein activation
07:53

A Fluorogenic Peptide Cleavage Assay to Screen for Proteolytic Activity: Applications for coronavirus spike protein activation

Published on: January 9, 2019

Alphavirus structure: activation for entry at the target cell surface.

Marie-Christine Vaney1, Stéphane Duquerroy, Félix A Rey

  • 1Institut Pasteur, Unité de Virologie Structurale, CNRS UMR 3569, Paris, France.

Current Opinion in Virology
|April 30, 2013
PubMed
Summary
This summary is machine-generated.

Recent advances reveal the 3D structure of alphavirus particles, detailing glycoprotein complexes and virion organization. This provides new insights into virus entry and glycoprotein shell disassembly.

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Area of Science:

  • Virology
  • Structural Biology
  • Biophysics

Background:

  • Alphavirus particles possess a complex 3D organization.
  • Understanding this structure is key to deciphering viral mechanisms.

Purpose of the Study:

  • To review recent discoveries in alphavirus particle 3D organization.
  • To discuss implications for viral entry and disassembly.

Main Methods:

  • Crystal structures of envelope glycoprotein complexes.
  • Electron microscopy reconstructions of intact virions.

Main Results:

  • High-resolution (7Å–4Å) structural data of alphavirus virions.
  • Detailed description of glycoprotein shell organization at neutral and acidic pH.

Conclusions:

  • New structural data offers unprecedented detail on alphavirus virions.
  • Insights into the mechanism of alphavirus entry and glycoprotein shell disassembly.
  • Identifies key outstanding questions in alphavirus structural biology.