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

Inhibitors Of Virion Release

Inhibitors Of Virion Release

Viral replication and dissemination rely on efficient mechanisms for host cell entry, genome replication, assembly, and release. Influenza viruses, such as types A and B, are negative-sense single-stranded RNA viruses with a segmented genome, that depend on two critical surface glycoproteins to carry out these processes: hemagglutinin (HA) and neuraminidase (NA). HA initiates infection by binding to sialic acid residues on the surface of host epithelial cells, facilitating receptor-mediated...

Inhibitors of Virion Maturation and Assembly

Inhibitors of Virion Maturation and Assembly

As part of their replication cycle, certain viruses synthesize long precursor proteins called polyproteins within infected host cells. In human immunodeficiency virus (HIV), two major polyproteins are produced: Gag and Gag-Pol. The Gag polyprotein supplies the structural components of the virus, while Gag-Pol includes essential viral enzymes such as reverse transcriptase, integrase, and protease. After synthesis, these polyproteins move to the host cell membrane, where they assemble into an...

Inhibitors of Viral Protein Synthesis

Inhibitors of Viral Protein Synthesis

Protein synthesis is indispensable for viral replication, as viruses lack the cellular machinery required for this process and must hijack the host's translational apparatus. In response, host cells deploy a critical innate immune defense involving interferons, specialized cytokines that play a central role in inhibiting viral propagation.Upon viral detection, infected cells release interferons that bind to receptors on adjacent uninfected cells, activating the JAK-STAT signaling pathway and...

Fusion of Secretory Vesicles with the Plasma Membrane

Fusion of Secretory Vesicles with the Plasma Membrane

Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...

Pinching-off of Coated Vesicles

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...

SNAREs and Membrane Fusion

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...

You might also read

Related Articles

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

Sort by

Same author

Prognostic value of circulating tumor DNA in pancreatic cancer: a systematic review and meta-analysis.

Aging·2020

Same author

The role of ferroptosis regulators in the prognosis, immune activity and gemcitabine resistance of pancreatic cancer.

Annals of translational medicine·2020

Same author

The vascular endothelial growth factor trap aflibercept induces vascular dysfunction and hypertension via attenuation of eNOS/NO signaling in mice.

Acta pharmacologica Sinica·2020

Same author

MBNL1 regulates isoproterenol-induced myocardial remodelling in vitro and in vivo.

Journal of cellular and molecular medicine·2020

Same author

Platelets Stimulate Liver Regeneration in a Rat Model of Partial Liver Transplantation.

Liver transplantation : official publication of the American Association for the Study of Liver Diseases and the International Liver Transplantation Society·2020

Same author

Mutant p53 in Cancer Progression and Targeted Therapies.

Frontiers in oncology·2020

Search research articles

Related Experiment Video

Updated: Jun 2, 2026

Engineering Antiviral Agents via Surface Plasmon Resonance

Engineering Antiviral Agents via Surface Plasmon Resonance

Published on: June 14, 2022

Tetherin inhibits prototypic foamy virus release.

Fengwen Xu¹, Juan Tan, Ruikang Liu

¹Key Laboratory of Molecular Microbiology and Biotechnology (Ministry of Education) and Key Laboratory of Microbial Functional Genomics (Tianjin), College of Life Sciences, Nankai University, Tianjin 300071, China.

Virology Journal

|May 3, 2011

Summary

Tetherin protein restricts enveloped virus release, including foamy viruses (PFV). Human immunodeficiency virus type 1 (HIV-1) Vpu protein counteracts this restriction, with tetherin

More Related Videos

Production of Pseudotyped Particles to Study Highly Pathogenic Coronaviruses in a Biosafety Level 2 Setting

Production of Pseudotyped Particles to Study Highly Pathogenic Coronaviruses in a Biosafety Level 2 Setting

Published on: March 1, 2019

Two Methods of Heterokaryon Formation to Discover HCV Restriction Factors

Two Methods of Heterokaryon Formation to Discover HCV Restriction Factors

Published on: July 16, 2012

Related Experiment Videos

Last Updated: Jun 2, 2026

Engineering Antiviral Agents via Surface Plasmon Resonance

Engineering Antiviral Agents via Surface Plasmon Resonance

Published on: June 14, 2022

Production of Pseudotyped Particles to Study Highly Pathogenic Coronaviruses in a Biosafety Level 2 Setting

Production of Pseudotyped Particles to Study Highly Pathogenic Coronaviruses in a Biosafety Level 2 Setting

Published on: March 1, 2019

Two Methods of Heterokaryon Formation to Discover HCV Restriction Factors

Two Methods of Heterokaryon Formation to Discover HCV Restriction Factors

Published on: July 16, 2012

Area of Science:

Virology
Immunology

Background:

Tetherin (BST-2, CD317, HM1.24) is an interferon-induced antiviral protein.
Tetherin blocks the release of various enveloped viruses like retroviruses, filoviruses, and herpesviruses.
The interaction between tetherin and foamy viruses remained unclear.

Purpose of the Study:

To investigate the role of tetherin in foamy virus (PFV) production.
To determine if HIV-1 Vpu antagonizes tetherin's effect on PFV.
To elucidate the structural requirements of tetherin for PFV inhibition.

Main Methods:

Assessed tetherin's inhibition of prototypic foamy virus (PFV) production across species.
Investigated the counteraction of human tetherin by HIV-1 Vpu.
Generated and analyzed tetherin mutants (transmembrane domain deletion, GPI anchor deletion, dimerization-deficient, glycosylation-deficient).

Main Results:

Tetherin from human, simian, bovine, and canine origins inhibited infectious PFV production.
HIV-1 Vpu counteracted the inhibitory effect of human tetherin on PFV.
Transmembrane domain and GPI anchor deletion mutants showed moderate inhibition of PFV, while dimerization and glycosylation deficient mutants were as effective as wild-type tetherin.

Conclusions:

Tetherin effectively inhibits PFV release and infectivity.
HIV-1 Vpu antagonizes tetherin-mediated inhibition of PFV.
Tetherin's transmembrane domain and GPI anchor are crucial for PFV inhibition, but dimerization and glycosylation are not essential.