Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Coronavirus01:29

Coronavirus

Coronaviruses, including the severe acute respiratory syndrome coronavirus (SARS-CoV), are enveloped viruses characterized by their single-stranded, positive-sense RNA genome and helical nucleocapsid structure. The hallmark of these viruses is their club-shaped spike (S) glycoproteins that protrude from the viral envelope, facilitating attachment to host cells. Typically, coronaviruses infect the upper respiratory tract, often causing mild or asymptomatic disease. However, certain strains like...
Viruses with RNA Genomes01:29

Viruses with RNA Genomes

RNA viruses are categorized into positive-strand, negative-strand, or double-stranded groups based on their genomic structure and replication mechanisms. This classification dictates how they exploit host cellular machinery for protein synthesis and replication. Some RNA viruses also utilize reverse transcription as part of their life cycle, further diversifying their replication strategies.Positive-Strand RNA VirusesPositive-strand RNA viruses have genomes that function directly as messenger...
Leaky Scanning02:28

Leaky Scanning

During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R stands for...
Inhibitors of Virion Maturation and Assembly01:19

Inhibitors of Virion Maturation and Assembly

As part of their replication cycle, certain viruses synthesize long precursor proteins called polyproteins within infected host cells. In human immunodeficiency virus (HIV), two major polyproteins are produced: Gag and Gag-Pol. The Gag polyprotein supplies the structural components of the virus, while Gag-Pol includes essential viral enzymes such as reverse transcriptase, integrase, and protease. After synthesis, these polyproteins move to the host cell membrane, where they assemble into an...
Protein Complex Assembly02:41

Protein 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...
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.

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Enhancing the Outcome of Crystallographic Fragment Screening by Choosing the Optimal Protein Crystal Form.

Small science·2026
Same author

Why is the Omicron main protease of SARS-CoV-2 less stable than its wild-type counterpart? A crystallographic, biophysical, and theoretical study.

hLife·2026
Same author

Thiazolyl 4-carboxylate ketone as a new warhead for a highly potent SARS-CoV-2 main protease inhibitor.

European journal of medicinal chemistry·2025
Same author

Rolf Peter Hilgenfeld (1954-2025).

Acta crystallographica. Section D, Structural biology·2025
Same author

A coronavirus assembly inhibitor that targets the viral membrane protein.

Nature·2025
Same author

Structure-Based Optimization of Pyridone α-Ketoamides as Inhibitors of the SARS-CoV-2 Main Protease.

Journal of medicinal chemistry·2025

Related Experiment Video

Updated: Jul 2, 2026

Engineering Antiviral Agents via Surface Plasmon Resonance
13:00

Engineering Antiviral Agents via Surface Plasmon Resonance

Published on: June 14, 2022

Variable oligomerization modes in coronavirus non-structural protein 9.

Rajesh Ponnusamy1, Ralf Moll, Thomas Weimar

  • 1Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany.

Journal of Molecular Biology
|August 13, 2008
PubMed
Summary

Human coronavirus 229E non-structural protein 9 (Nsp9) forms a unique disulfide-linked dimer, differing from SARS-CoV Nsp9. This structural variation impacts RNA binding and aggregation, suggesting biological relevance under oxidative stress.

More Related Videos

Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus
09:08

Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus

Published on: July 27, 2021

Production of Pseudotyped Particles to Study Highly Pathogenic Coronaviruses in a Biosafety Level 2 Setting
08:40

Production of Pseudotyped Particles to Study Highly Pathogenic Coronaviruses in a Biosafety Level 2 Setting

Published on: March 1, 2019

Related Experiment Videos

Last Updated: Jul 2, 2026

Engineering Antiviral Agents via Surface Plasmon Resonance
13:00

Engineering Antiviral Agents via Surface Plasmon Resonance

Published on: June 14, 2022

Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus
09:08

Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus

Published on: July 27, 2021

Production of Pseudotyped Particles to Study Highly Pathogenic Coronaviruses in a Biosafety Level 2 Setting
08:40

Production of Pseudotyped Particles to Study Highly Pathogenic Coronaviruses in a Biosafety Level 2 Setting

Published on: March 1, 2019

Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • Non-structural protein 9 (Nsp9) is crucial for coronavirus replication, binding single-stranded RNA.
  • Previous studies on SARS-CoV Nsp9 revealed its dimeric structure.
  • The structural and functional characteristics of HCoV-229E Nsp9 were not fully understood.

Purpose of the Study:

  • To determine the crystal structure of HCoV-229E Nsp9.
  • To investigate the structural differences between HCoV-229E Nsp9 and SARS-CoV Nsp9.
  • To elucidate the role of Nsp9 structure in single-stranded RNA binding.

Main Methods:

  • X-ray crystallography to determine Nsp9 structures (wild-type and Cys69Ala mutant).
  • Chemical cross-linking to assess protein aggregation in solution.
  • Zone-interference gel electrophoresis and surface plasmon resonance to evaluate nucleic acid binding affinity.

Main Results:

  • HCoV-229E Nsp9 forms a novel disulfide-linked homodimer, distinct from SARS-CoV Nsp9.
  • Mutating Cys69 in HCoV-229E Nsp9 resulted in a dimer organization similar to SARS-CoV Nsp9.
  • Wild-type HCoV-229E Nsp9 exhibited higher affinity for oligonucleotides than its mutants, unlike SARS-CoV Nsp9 mutants.
  • Crystal structures revealed distinct aggregation patterns: trimers of dimers for wild-type HCoV-229E Nsp9 and rod-like polymers for the mutant and SARS-CoV Nsp9.

Conclusions:

  • HCoV-229E Nsp9 possesses a unique disulfide-linked dimeric structure that influences its RNA-binding properties.
  • Both disulfide-linked and non-disulfide-linked Nsp9 dimers may be biologically relevant.
  • The disulfide-bonded Nsp9 dimer formation could be linked to oxidative stress during viral infection.