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

SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

13.6K
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...
13.6K
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

3.8K
Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
3.8K
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

4.1K
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
4.1K
Size and Structure of Viral Genomes01:26

Size and Structure of Viral Genomes

1.1K
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...
1.1K
Protein-protein Interfaces02:04

Protein-protein Interfaces

15.0K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
15.0K
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

4.7K
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...
4.7K

You might also read

Related Articles

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

Sort by
Same author

Engineering B cells to express fully customizable antibodies with enhanced Fc functions.

Nature communications·2026
Same author

Unveiling alternate pathways for SARS-CoV-2 infection via extracellular vesicle-mediated transfer of ACE2 and TMPRSS2.

Nature communications·2026
Same author

Preclinical efficacy and safety assessment of engineered regulatory T cells for treatment of IPEX and other autoimmune disorders.

Molecular therapy : the journal of the American Society of Gene Therapy·2026
Same author

Overcoming barriers to commercially pre-viable gene and cell therapies for rare and ultra-rare diseases.

Molecular therapy : the journal of the American Society of Gene Therapy·2025
Same author

Engineering B cells to Express Fully Customizable Antibodies with Enhanced Fc Functions.

bioRxiv : the preprint server for biology·2025
Same author

Reprogramming human B cells with custom heavy-chain antibodies.

Nature biomedical engineering·2024

Related Experiment Video

Updated: Apr 5, 2026

Imaging of HIV-1 Envelope-induced Virological Synapse and Signaling on Synthetic Lipid Bilayers
11:45

Imaging of HIV-1 Envelope-induced Virological Synapse and Signaling on Synthetic Lipid Bilayers

Published on: March 8, 2012

12.8K

Determinants in HIV-2 Env and tetherin required for functional interaction.

Colin M Exline1, Su Jung Yang2, Kevin G Haworth3

  • 1Department of Molecular Microbiology and Immunology, Keck School of Medicine, University of Southern California, 2011 Zonal Avenue, HMR 502, Los Angeles, CA, 90033, USA. colinexline@gmail.com.

Retrovirology
|August 8, 2015
PubMed
Summary

Human immunodeficiency virus type 2 (HIV-2) Env protein counteracts BST-2/tetherin by physically interacting with it. This interaction is crucial for viral release, and HIV-2 maintains strong selective pressure to preserve this anti-tetherin activity.

More Related Videos

Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay
07:10

Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay

Published on: September 14, 2014

14.8K
Identification of Nucleolar Factors During HIV-1 Replication Through Rev Immunoprecipitation and Mass Spectrometry
09:38

Identification of Nucleolar Factors During HIV-1 Replication Through Rev Immunoprecipitation and Mass Spectrometry

Published on: June 26, 2019

8.7K

Related Experiment Videos

Last Updated: Apr 5, 2026

Imaging of HIV-1 Envelope-induced Virological Synapse and Signaling on Synthetic Lipid Bilayers
11:45

Imaging of HIV-1 Envelope-induced Virological Synapse and Signaling on Synthetic Lipid Bilayers

Published on: March 8, 2012

12.8K
Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay
07:10

Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay

Published on: September 14, 2014

14.8K
Identification of Nucleolar Factors During HIV-1 Replication Through Rev Immunoprecipitation and Mass Spectrometry
09:38

Identification of Nucleolar Factors During HIV-1 Replication Through Rev Immunoprecipitation and Mass Spectrometry

Published on: June 26, 2019

8.7K

Area of Science:

  • Virology
  • Immunology
  • Molecular Biology

Background:

  • BST-2/tetherin is an interferon-inducible protein that restricts the release of enveloped viruses.
  • Primate lentiviruses, including HIV-2, have developed mechanisms to overcome tetherin restriction.
  • The HIV-2 Env protein is known to counteract tetherin, but the specific features involved are not fully understood.

Purpose of the Study:

  • To elucidate the molecular interactions between HIV-2 Env and BST-2/tetherin.
  • To identify the specific domains and residues critical for this interaction and counteraction.
  • To evaluate the evolutionary pressure on HIV-2 to maintain anti-tetherin activity.

Main Methods:

  • Analysis of HIV-2 Env mutants with alterations in the ectodomain and cytoplasmic tail.
  • Construction of artificial tetherin-like proteins to test domain function.
  • Viral replication assays and genetic passaging experiments.

Main Results:

  • A physical interaction between HIV-2 Env and tetherin is essential for counteracting tetherin.
  • This interaction maps to the ectodomains of both proteins, requiring specific alanine residues in tetherin.
  • Mutations impairing this interaction slowed viral replication, but compensatory mutations arose in the Env cytoplasmic tail, restoring function.

Conclusions:

  • The interaction between HIV-2 Env and tetherin is a direct physical one, primarily involving their ectodomains.
  • There is significant evolutionary pressure on HIV-2 to maintain the ability of its Env protein to counteract tetherin.
  • Understanding this interaction provides insights into lentiviral evasion strategies.