Related Experiment Video
Updated: May 28, 2026
09:08
Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus
Published on: July 27, 2021
Structure of the vesicular stomatitis virus N⁰-P complex
Cédric Leyrat1, Filip Yabukarski, Nicolas Tarbouriech
1UMI 3265 UJF-EMBL-CNRS Unit of Virus Host Cell Interactions, Grenoble, France.
Plos Pathogens
|October 1, 2011
Summary
Replication of RNA viruses needs nucleoprotein (N) and phosphoprotein (P). We structurally characterized an N-P complex, revealing how P binding inhibits N polymerization, aiding viral RNA synthesis initiation.
Area of Science:
- Virology
- Structural Biology
- Biochemistry
Background:
- Non-segmented negative-strand RNA virus replication depends on nucleoprotein (N) and phosphoprotein (P) complexes.
- The interaction between N and P is crucial for viral RNA synthesis.
Purpose of the Study:
- To structurally characterize a soluble heterodimeric complex of vesicular stomatitis virus N (N(Δ21)) and a phosphoprotein peptide (P(60)).
- To elucidate the mechanism by which P(60) binding to N(0) inhibits RNA binding and N polymerization.
Main Methods:
- X-ray crystallography (3.0 Å resolution) to determine the complex structure.
- Small-angle X-ray scattering (SAXS) and NMR spectroscopy to confirm binding and flexibility.
Main Results:
- The complex formed a decameric circular structure.
- The P(60) molecular recognition element (MoRE) folds upon binding to N(Δ21), competing with RNA binding.
- SAXS and NMR confirmed MoRE binding and flexibility in flanking regions.
Conclusions:
- The structure provides insights into how P binding regulates N polymerization.
- This complex structure suggests a mechanism for the initiation of viral RNA synthesis.
More Related Videos
08:40Production of Pseudotyped Particles to Study Highly Pathogenic Coronaviruses in a Biosafety Level 2 Setting
Published on: March 1, 2019
09:13Using Reverse Genetics to Manipulate the NSs Gene of the Rift Valley Fever Virus MP-12 Strain to Improve Vaccine Safety and Efficacy
Published on: November 1, 2011
Related Concept Videos
00:56Viral 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.
02:41Protein Complex Assembly
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
01:33Coat 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...
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...
01:12Clathrin Coated Vesicles
Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
00:59COP Coated Vesicles
Membrane-enclosed structures called vesicles transport proteins and lipids across the cell. The vesicles derive their cargo from the plasma membrane, Golgi, ER, or endosome. Coated vesicles are spherical, protein-coated carriers with a 50–100 nm diameter that mediate bidirectional transport between the ER and the Golgi. The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. Their formation is driven by the assembly of different...
01:32Pinching-off of Coated Vesicles
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...