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Related Concept Videos

Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...

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Related Experiment Video

Updated: May 20, 2026

Nucleocapsid Annealing-Mediated Electrophoresis (NAME) Assay Allows the Rapid Identification of HIV-1 Nucleocapsid Inhibitors
08:33

Nucleocapsid Annealing-Mediated Electrophoresis (NAME) Assay Allows the Rapid Identification of HIV-1 Nucleocapsid Inhibitors

Published on: January 19, 2015

SNAREs in HIV-1 assembly.

Himanshu Garg1, Anjali Joshi

  • 1Center of Excellence for Infectious Diseases; Department of Biomedical Sciences; Paul L. Foster School of Medicine; Texas Tech University Health Sciences Center; El Paso, TX USA.

Communicative & Integrative Biology
|July 19, 2012
PubMed
Summary

Disrupting host SNARE proteins impacts HIV-1 assembly by altering Gag protein localization. Further research is needed to clarify if this effect stems from general cellular disruption or specific SNARE interactions.

Keywords:
GagHIV-1NSFSNAREsbuddingdominant negativevirus assembly

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Last Updated: May 20, 2026

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08:33

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Published on: January 19, 2015

Visualization of HIV-1 Gag Binding to Giant Unilamellar Vesicle (GUV) Membranes
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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

Area of Science:

  • Virology
  • Cell Biology
  • Molecular Biology

Background:

  • Enveloped viruses rely on host factors for replication, particularly during assembly and budding.
  • Host SNARE proteins mediate vesicular transport, crucial for protein trafficking and membrane fusion.
  • Previous studies indicated SNARE disruption affects HIV-1 assembly and Gag protein localization.

Purpose of the Study:

  • To investigate the specific role of host SNARE proteins in HIV-1 assembly.
  • To determine if observed effects are due to general cellular disruption or specific SNARE involvement.
  • To differentiate the roles of "v" and "t" SNAREs in the HIV-1 budding process.

Main Methods:

  • Generalized disruption of the SNARE sorting machinery.
  • Analysis of Gag protein localization to the plasma membrane in HIV-1 infected cells.

Main Results:

  • Generalized disruption of SNARE proteins affected Gag localization to the plasma membrane.
  • This suggests a role for SNARE proteins in HIV-1 assembly.

Conclusions:

  • Host SNARE proteins are implicated in HIV-1 assembly.
  • Further studies are required to elucidate the precise mechanisms and specific SNARE involvement.