Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Coronavirus

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...

You might also read

Related Articles

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

Sort by

Same author

Genome evolution in parthenogenetic nematodes shaped by chromosome rearrangements and introgression.

Genome research·2026

Same author

LGL-1 and the RhoGAP protein PAC-1 redundantly polarize the Caenorhabditis elegans embryonic epidermis.

The Journal of cell biology·2026

Same author

Arsenite methyltransferase 3 is required for mitochondrial function and hepatic lipid metabolism.

The FEBS journal·2026

Same author

Manganese-Templated Nontrivial Structures for MRI and Therapy.

Journal of the American Chemical Society·2026

Same author

LGL-1 and the RhoGAP protein PAC-1 redundantly polarize the <i>C. elegans</i> embryonic epidermis.

bioRxiv : the preprint server for biology·2026

Same author

Structural characterization and thermodynamic behavior of melittin-derived peptide interactions with gram-positive bacterial cell membranes using molecular dynamics simulation.

RSC advances·2026

Search research articles

Related Experiment Video

Updated: Jun 19, 2026

A Liquid Phase Affinity Capture Assay Using Magnetic Beads to Study Protein-Protein Interaction: The Poliovirus-Nanobody Example

A Liquid Phase Affinity Capture Assay Using Magnetic Beads to Study Protein-Protein Interaction: The Poliovirus-Nanobody Example

Published on: May 29, 2012

Assessing nanobody interaction with SARS-CoV-2 Nsp9.

Gennaro Esposito^1,2, Yamanappa Hunashal¹, Mathias Percipalle¹

¹Division of Science, New York University Abu Dhabi, Abu Dhabi, UAE.

|May 17, 2024

Summary

Researchers used NMR spectroscopy to study SARS-CoV-2 Nsp9 protein interactions with nanobody 2NSP90. This interaction is a potential antiviral target, as Nsp9 is crucial for viral replication across coronaviruses.

More Related Videos

Detection of SARS-CoV-2 Neutralizing Antibodies using High-Throughput Fluorescent Imaging of Pseudovirus Infection

Detection of SARS-CoV-2 Neutralizing Antibodies using High-Throughput Fluorescent Imaging of Pseudovirus Infection

Published on: June 5, 2021

Engineering Antiviral Agents via Surface Plasmon Resonance

Engineering Antiviral Agents via Surface Plasmon Resonance

Published on: June 14, 2022

Related Experiment Videos

Last Updated: Jun 19, 2026

A Liquid Phase Affinity Capture Assay Using Magnetic Beads to Study Protein-Protein Interaction: The Poliovirus-Nanobody Example

A Liquid Phase Affinity Capture Assay Using Magnetic Beads to Study Protein-Protein Interaction: The Poliovirus-Nanobody Example

Published on: May 29, 2012

Detection of SARS-CoV-2 Neutralizing Antibodies using High-Throughput Fluorescent Imaging of Pseudovirus Infection

Detection of SARS-CoV-2 Neutralizing Antibodies using High-Throughput Fluorescent Imaging of Pseudovirus Infection

Published on: June 5, 2021

Engineering Antiviral Agents via Surface Plasmon Resonance

Engineering Antiviral Agents via Surface Plasmon Resonance

Published on: June 14, 2022

Area of Science:

Structural biology
Virology
Biochemistry

Background:

SARS-CoV-2 non-structural protein 9 (Nsp9) is vital for viral replication and transcription.
Nsp9's conserved nature across coronaviruses makes it a promising antiviral target.
Nanobodies offer a potential strategy to inhibit Nsp9 function.

Purpose of the Study:

To investigate the interaction between SARS-CoV-2 Nsp9 and nanobody 2NSP90 using NMR spectroscopy.
To determine the stoichiometry and epitope mapping of the Nsp9-nanobody complex.
To reconcile NMR findings with existing structural data.

Main Methods:

Nuclear Magnetic Resonance (NMR) spectroscopy with paramagnetic perturbation (PENELOP).
Molecular dynamics (MD) simulations.
Analysis of Nsp9 oligomerization states (dimers and tetramers).

Main Results:

NMR data suggest a 4:4 Nsp9-to-nanobody stoichiometry with specific epitope pairs.
MD simulations indicate both Nsp9 dimers and tetramers are plausible oligomeric states.
NMR experiments ruled out a conformational change in Nsp9 observed in a crystal structure of a similar complex.

Conclusions:

The study provides detailed insights into the solution-state structure of the Nsp9-nanobody complex.
NMR findings challenge certain aspects of previously reported crystal structures regarding Nsp9 conformation.
Understanding these interactions is key for developing broad-spectrum coronavirus antivirals targeting Nsp9.