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

Membrane Fluidity01:26

Membrane Fluidity

Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
Mosaic nature of the membrane
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is a relatively...
SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
Rab Proteins01:14

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...
Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
Asymmetric Lipid Bilayer01:35

Asymmetric Lipid Bilayer

Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...

You might also read

Related Articles

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

Sort by
Same author

Structures of folding intermediates on BAM show diverse substrates fold by a conserved mechanism.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Establishment of a Neonatal Natural Transmission Model for CMV Vaccine Development.

The Journal of infectious diseases·2026
Same author

Mechanism of membrane perforation in rotavirus cell entry.

bioRxiv : the preprint server for biology·2026
Same author

Structures of folding intermediates on BAM show diverse substrates fold by a uniform mechanism.

bioRxiv : the preprint server for biology·2025
Same author

Dynamics of Respiratory Syncytial Virus Illness and Serology During Pregnancy and Infancy in the United States and South Africa.

Open forum infectious diseases·2025
Same author

Author Correction: BNT162b2 vaccine induces neutralizing antibodies and poly-specific T cells in humans.

Nature·2025

Related Experiment Video

Updated: Jun 17, 2026

Assays for the Specific Growth Rate and Cell-binding Ability of Rotavirus
10:49

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

Published on: January 28, 2019

A rotavirus spike protein conformational intermediate binds lipid bilayers.

Shane D Trask1, Irene S Kim, Stephen C Harrison

  • 1Laboratory of Molecular Medicine, Children's Hospital, Boston, Massachusetts 02115, USA.

Journal of Virology
|December 17, 2009
PubMed
Summary

Rotavirus protein VP5 binds to host cell membranes during viral entry. This binding occurs when VP5 undergoes a conformational change, similar to fusion proteins in enveloped viruses.

More Related Videos

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
09:49

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

Published on: April 2, 2015

Simplified Reverse Genetics Method to Recover Recombinant Rotaviruses Expressing Reporter Proteins
11:40

Simplified Reverse Genetics Method to Recover Recombinant Rotaviruses Expressing Reporter Proteins

Published on: April 17, 2020

Related Experiment Videos

Last Updated: Jun 17, 2026

Assays for the Specific Growth Rate and Cell-binding Ability of Rotavirus
10:49

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

Published on: January 28, 2019

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
09:49

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

Published on: April 2, 2015

Simplified Reverse Genetics Method to Recover Recombinant Rotaviruses Expressing Reporter Proteins
11:40

Simplified Reverse Genetics Method to Recover Recombinant Rotaviruses Expressing Reporter Proteins

Published on: April 17, 2020

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Rotavirus, a common cause of gastroenteritis, enters host cells by penetrating the cell membrane.
  • The outer capsid protein VP4 is cleaved into VP5 and VP8 during entry.
  • VP5 is hypothesized to mediate membrane interaction during rotavirus uncoating.

Purpose of the Study:

  • To provide direct experimental evidence for VP5-mediated membrane binding during rotavirus entry.
  • To investigate the conformational changes of VP5 and their role in membrane association.
  • To understand the mechanism of VP5 interaction with lipid bilayers.

Main Methods:

  • Liposome binding assays with intact and uncoated rotavirus virions.
  • Conformational studies of VP5 using EDTA-triggered rearrangement.
  • Analysis of a VP5 fragment (VP5CT) interaction with liposomes.
  • Neutralizing antibody inhibition assays.

Main Results:

  • VP5 binds to liposomes only when rearrangement is triggered in their presence, not when pre-formed or in intact virions.
  • Liposomes enhance the VP5 conformational change during rearrangement.
  • A VP5 fragment also binds liposomes during proteolysis in their presence.
  • A neutralizing antibody blocks VP5 liposome association, indicating its role in entry.

Conclusions:

  • Rotavirus VP5 binds lipid bilayers in an intermediate conformational state during viral entry.
  • This binding mechanism is analogous to fusion proteins of enveloped viruses.
  • VP5 rearrangement is a critical step for membrane interaction and subsequent viral entry.