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

Mismatch Repair01:36

Mismatch Repair

Overview
Viral Recombination00:57

Viral Recombination

Cells are sometimes infected by more than one virus at once. When two viruses disassemble to expose their genomes for replication in the same cell, similar regions of their genomes can pair together and exchange sequences in a process called recombination. Alternatively, viruses with segmented genomes can swap segments in a process called reassortment.
Viral Mutations00:36

Viral Mutations

A mutation is a change in the sequence of bases of DNA or RNA in a genome. Some mutations occur during replication of the genome due to errors made by the polymerase enzymes that replicate DNA or RNA. Unlike DNA polymerase, RNA polymerase is prone to errors because it is not capable of “proofreading” its work. Viruses with RNA-based genomes, like HIV, therefore accrue mutations faster than viruses with DNA-based genomes. Because mutation and recombination provide the raw material for adaptive...
Single Nucleotide Polymorphisms-SNPs01:05

Single Nucleotide Polymorphisms-SNPs

A single nucleotide polymorphism or SNP is a single nucleotide variation at a specific genomic position in a large population. It is the most prevalent type of sequence variation found in the human genome. Point mutations that occur in more than 1% of the population qualify as SNPs. These are present once every 1000 nucleotides on an average in the human genome. Replacement of a purine with another purine (A/G) or a pyrimidine with another pyrimidine (C/T) is known as a transition. In contrast,...
Mismatch Repair01:20

Mismatch Repair

Organisms are capable of detecting and fixing nucleotide mismatches that occur during DNA replication. This sophisticated process requires identifying the new strand and replacing the erroneous bases with correct nucleotides. Mismatch repair is coordinated by many proteins in both prokaryotes and eukaryotes.
The Mutator Protein Family Plays a Key Role in DNA Mismatch Repair
The human genome has more than 3 billion base pairs of DNA per cell. Prior to cell division, that vast amount of genetic...
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...

You might also read

Related Articles

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

Sort by
Same author

Applying Distinct CDMS Strategies to Observe Nonclassical Virus Capsid Assembly.

Journal of mass spectrometry : JMS·2026
Same author

Native mass spectrometry meets X-rays for the elucidation of protein structures.

Biochemical Society transactions·2026
Same author

Molecular action of NZ2114, a superior plectasin derivative.

npj antimicrobials and resistance·2026
Same author

Statistical crystallography reveals an allosteric network in SARS-CoV-2 M<sup>pro</sup>.

Communications biology·2026
Same author

Dynamics of viral self-assembly, viral genome packaging, and virus-cell interactions studied by optical tweezers.

European biophysics journal : EBJ·2026
Same author

MDA5 generates compact ribonucleoprotein complexes via ATP-dependent double-stranded RNA unwinding.

Nucleic acids research·2026

Related Experiment Video

Updated: Jul 24, 2026

Production of Human Norovirus Protruding Domains in E. coli for X-ray Crystallography
10:46

Production of Human Norovirus Protruding Domains in E. coli for X-ray Crystallography

Published on: April 19, 2016

8.7K

Fucose Binding Cancels out Mechanical Differences between Distinct Human Noroviruses.

Yuzhen Feng1, Ronja Pogan2,3, Lars Thiede2,3

  • 1Moleculaire Biofysica, Zernike Instituut, Rijksuniversiteit Groningen, 9747AG Groningen, The Netherlands.

Viruses
|July 29, 2023
PubMed
Summary

Norovirus variants show different mechanical properties, but fucose binding reduces these differences. This suggests a dynamic capsid mechanism that may enhance norovirus infection and prevalence.

Keywords:
AFMmechanical propertiesnanoindentationnorovirus-like particles (noroVLPs)virus-ligand interaction

More Related Videos

Alternative In Vitro Methods for the Determination of Viral Capsid Structural Integrity
12:57

Alternative In Vitro Methods for the Determination of Viral Capsid Structural Integrity

Published on: November 16, 2017

8.2K
Quantifying Human Norovirus Virus-like Particles Binding to Commensal Bacteria Using Flow Cytometry
07:02

Quantifying Human Norovirus Virus-like Particles Binding to Commensal Bacteria Using Flow Cytometry

Published on: April 29, 2020

8.0K

Related Experiment Videos

Last Updated: Jul 24, 2026

Production of Human Norovirus Protruding Domains in E. coli for X-ray Crystallography
10:46

Production of Human Norovirus Protruding Domains in E. coli for X-ray Crystallography

Published on: April 19, 2016

8.7K
Alternative In Vitro Methods for the Determination of Viral Capsid Structural Integrity
12:57

Alternative In Vitro Methods for the Determination of Viral Capsid Structural Integrity

Published on: November 16, 2017

8.2K
Quantifying Human Norovirus Virus-like Particles Binding to Commensal Bacteria Using Flow Cytometry
07:02

Quantifying Human Norovirus Virus-like Particles Binding to Commensal Bacteria Using Flow Cytometry

Published on: April 29, 2020

8.0K

Area of Science:

  • Virology
  • Biophysics
  • Structural Biology

Background:

  • Noroviruses cause widespread gastroenteritis in humans and livestock.
  • Frequent mutations lead to diverse norovirus variants with strain-dependent binding characteristics.
  • The molecular mechanisms underlying strain-dependent norovirus function remain largely unknown.

Purpose of the Study:

  • To investigate the molecular mechanism behind strain-dependent norovirus functioning.
  • To explore the relationship between viral mechanical properties and norovirus variants.
  • To understand how norovirus capsids adapt to environmental changes.

Main Methods:

  • Utilized atomic force microscopy (AFM) nanoindentation technology.
  • Studied norovirus-like particles (noroVLPs) from three distinct human norovirus variants.
  • Analyzed changes in viral mechanical properties after fucose treatment.

Main Results:

  • Significant differences in viral mechanical properties were observed among norovirus variants, even within the same genogroup.
  • Fucose treatment surprisingly diminished the previously identified mechanical property differences.
  • A dynamic switch in the norovirus P domain upon fucose binding was proposed as the cause.

Conclusions:

  • Norovirus capsid mechanics are adaptable and influenced by fucose binding.
  • The dynamic P domain switch offers insights into norovirus adaptation and infection.
  • This study links viral mechanical properties to norovirus prevalence.