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

Leaky Scanning

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...

Rab Proteins

Rab Proteins

Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...

Viral Structure

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.

Size and Structure of Viral Genomes

Size and Structure of Viral Genomes

Viral genomes exhibit remarkable diversity in size, structure, and composition, influencing their replication strategies and interactions with host cells. These genomes consist of either DNA or RNA and may be linear or circular. Additionally, they can be single-stranded or double-stranded, with each configuration affecting how the virus propagates within a host. RNA viruses, for instance, generally have smaller genomes than DNA viruses, a factor that contributes to their high mutation rates and...

Protein Folding Quality Check in the RER

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...

You might also read

Related Articles

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

Sort by

Same author

Engineering a Novel Bacterial Encapsulin for Programmable Surface Functionalization: From Single-Target to Mosaic Nanovaccines.

bioRxiv : the preprint server for biology·2026

Same author

Age-related changes in visual performance: A defocus curve study in healthy phakic eyes.

PloS one·2026

Same author

Calicivirus assembly and stability are mediated by the N-terminal domain of the capsid protein with the involvement of the viral genome.

PLoS pathogens·2025

Same author

The upstream-downstream tension in the global health classroom.

BMJ global health·2025

Same author

Seroepidemiology of Human Non-Species A Rotavirus Infections in Valencia, Spain.

Journal of medical virology·2025

Same author

Structural determinants of rotavirus proteolytic activation.

bioRxiv : the preprint server for biology·2025

Search research articles

Related Experiment Video

Updated: Sep 11, 2025

Assays for the Specific Growth Rate and Cell-binding Ability of Rotavirus

Assays for the Specific Growth Rate and Cell-binding Ability of Rotavirus

Published on: January 28, 2019

Structural determinants of rotavirus proteolytic activation.

Dunia Asensio-Cob¹, Carlos P Mata², Josue Gomez-Blanco³

¹Department of Molecular Medicine, Peter Gilgan Centre for Research and Learning, The Hospital for Sick Children, Toronto, Ontario, Canada.

|August 12, 2025

Summary

Rotavirus (RV) infectivity requires trypsin-like proteases to activate its spike protein. Structural analysis reveals that surrounding loops constrain the spike, and their proteolysis releases this constraint for viral entry.

More Related Videos

Simplified Reverse Genetics Method to Recover Recombinant Rotaviruses Expressing Reporter Proteins

Simplified Reverse Genetics Method to Recover Recombinant Rotaviruses Expressing Reporter Proteins

Published on: April 17, 2020

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods

Published on: December 21, 2019

Related Experiment Videos

Last Updated: Sep 11, 2025

Assays for the Specific Growth Rate and Cell-binding Ability of Rotavirus

Assays for the Specific Growth Rate and Cell-binding Ability of Rotavirus

Published on: January 28, 2019

Simplified Reverse Genetics Method to Recover Recombinant Rotaviruses Expressing Reporter Proteins

Simplified Reverse Genetics Method to Recover Recombinant Rotaviruses Expressing Reporter Proteins

Published on: April 17, 2020

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods

Published on: December 21, 2019

Area of Science:

Virology
Structural Biology
Microbiology

Background:

Rotavirus (RV) is a major cause of severe childhood diarrhea.
RV infectivity depends on the proteolysis of its spike protein by host trypsin-like proteases.
Understanding RV spike protein activation is crucial for developing antiviral strategies.

Purpose of the Study:

To elucidate the structural basis of rotavirus spike protein activation by trypsin.
To investigate the conformational changes in the RV spike protein upon proteolysis.

Main Methods:

Cryogenic electron microscopy (cryo-EM) was employed to visualize RV particles.
Advanced image processing techniques were used for structural analysis.
Comparison of uncleaved and cleaved RV particles provided insights into conformational changes.

Main Results:

The uncleaved RV spike protein conformation is restricted by surrounding loops connecting the head to the body.
Proteolysis of these loops releases the structural constraint on the spike protein.
This release allows the spike protein to undergo conformational changes necessary for cell membrane penetration.

Conclusions:

Specific loops act as regulatory elements for rotavirus spike protein activation.
Proteolysis of these loops ensures timely activation of the spike protein for efficient viral infection.
The findings provide a structural understanding of rotavirus entry mechanism.