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

Acid Strength and Molecular Structure03:05

Acid Strength and Molecular Structure

33.1K
Binary Acids and Bases
In the absence of any leveling effect, the acid strength of binary compounds of hydrogen with nonmetals (A) increases as the H-A bond strength decreases down a group in the periodic table. For group 17, the order of increasing acidity is HF < HCl < HBr < HI. Likewise, for group 16, the order of increasing acid strength is H2O < H2S < H2Se < H2Te. Across a row in the periodic table, the acid strength of binary hydrogen compounds increases with increasing...
33.1K
Nucleic Acid Structure01:25

Nucleic Acid Structure

8.9K
The pentose sugar in DNA is deoxyribose, while in RNA the pentose sugar is ribose. The difference between the sugars is the presence of the hydroxyl group on the ribose's second carbon and a hydrogen on the deoxyribose's second carbon. The phosphate residue attaches to the hydroxyl group of the 5′ carbon of one sugar and the hydroxyl group of the 3′ carbon of the sugar of the next nucleotide, which forms  a 5′ to 3′ phosphodiester linkage.
DNA Structure
DNA...
8.9K
Molecular Structure and Acidity02:34

Molecular Structure and Acidity

20.9K
An acid can be deprotonated to form a conjugate base or an anion. If the produced anion is more stable, then the acid is stronger. On the contrary, if the anion is unstable, then the acid is weaker. Hence, to determine the acidity of the compound, the stability of its conjugate base is studied using various factors.
The size effect explains the change in atomic size on acidity. When comparing the acids formed from elements that belong to the same column in the periodic table, their atomic sizes...
20.9K
Viral Structure00:56

Viral Structure

74.5K
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.
74.5K
Bile01:19

Bile

4.2K
Bile is a crucial bodily fluid, characterized by its yellow-green color and alkaline nature. Produced in the liver, it is transported through the common hepatic duct into either the cystic duct, leading to the gallbladder, or directly into the common bile duct. The flow of bile is regulated by the sphincter of Oddi located at the entrance of the duodenum. When this sphincter is closed, bile is redirected to the gallbladder for storage and concentration.
Bile is released when dietary fats enter...
4.2K
Conserved Binding Sites01:49

Conserved Binding Sites

5.2K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
5.2K

You might also read

Related Articles

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

Sort by
Same author

Norovirus-specific monoclonal antibodies that block histo-blood group antigen binding isolated from healthy donors.

Journal of virology·2026
Same author

Harnessing marine sulfated polysaccharides to inhibit norovirus: from seaweed to solution.

Microbiology spectrum·2026
Same author

Structural insights into a broadly reactive nanobody that binds pathogenic and non-pathogenic lagoviruses.

Journal of virology·2026
Same author

Structural constraints prevent a bat norovirus from binding to histo-blood group antigen co-factors.

Journal of virology·2025
Same author

Antigenic structural analysis of bat and human norovirus protruding (P) domains.

Journal of virology·2025
Same author

Structural analysis of a non-pathogenic hare calicivirus capsid bound to a histo-blood group antigen co-factor.

Journal of virology·2024

Related Experiment Video

Updated: Feb 3, 2026

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

8.7K

Structural Basis for Human Norovirus Capsid Binding to Bile Acids.

Turgay Kilic1,2, Anna Koromyslova3,2, Grant S Hansman3,2

  • 1Schaller Research Group at the University of Heidelberg and the German Cancer Research Center, Heidelberg, Germany.

Journal of Virology
|October 26, 2018
PubMed
Summary

Bile acids are essential for the growth of some human noroviruses, acting as a cofactor by stabilizing capsid loops and enhancing histo-blood group antigen (HBGA) binding for specific genotypes.

Keywords:
X-ray crystallographynorovirusstructure

More Related Videos

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

8.5K
Using Multi-fluorinated Bile Acids and In Vivo Magnetic Resonance Imaging to Measure Bile Acid Transport
08:42

Using Multi-fluorinated Bile Acids and In Vivo Magnetic Resonance Imaging to Measure Bile Acid Transport

Published on: November 27, 2016

11.6K

Related Experiment Videos

Last Updated: Feb 3, 2026

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

8.7K
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

8.5K
Using Multi-fluorinated Bile Acids and In Vivo Magnetic Resonance Imaging to Measure Bile Acid Transport
08:42

Using Multi-fluorinated Bile Acids and In Vivo Magnetic Resonance Imaging to Measure Bile Acid Transport

Published on: November 27, 2016

11.6K

Area of Science:

  • Virology
  • Structural Biology
  • Biochemistry

Background:

  • Histo-blood group antigens (HBGAs) were previously the primary known cofactors for human norovirus infection.
  • Certain norovirus genotypes exhibit poor binding to HBGAs, suggesting the involvement of other factors.
  • Recent advancements in norovirus cell culture revealed bile's essential role in the growth of specific genotypes.

Purpose of the Study:

  • To investigate the interaction between human norovirus capsids and bile acids.
  • To understand the mechanism by which bile acids influence norovirus binding and infectivity.
  • To explore the cofactor role of bile acids in norovirus infection.

Main Methods:

  • Bile acid binding assays for various norovirus genotypes.
  • X-ray crystallography to determine the binding site of bile acids on norovirus capsids.
  • Amino acid sequence alignment and structural analysis to explain selective binding.

Main Results:

  • Bile acids demonstrated low-micromolar affinity for GII.1, GII.10, and GII.19 norovirus capsids, but not for GI.1, GII.3, GII.4, or GII.17.
  • X-ray crystallography revealed bile acid binding in a conserved pocket on the capsid's P domain.
  • Bile acid binding stabilized P domain loops, enabling HBGA binding in GII.1 (an HBGA nonbinder) and enhancing it in GII.10.

Conclusions:

  • Bile acids function as critical cofactors for certain human norovirus genotypes.
  • Bile acid binding acts as a regulator and enhancer of HBGA binding by stabilizing capsid structures.
  • The findings suggest a potential link between bile acid requirements and norovirus genotype prevalence and epidemic potential.