Hiv-1 Envelope Glycoproteins
Hiv-1 Envelope Glycoproteins - Related Videos
07:29
Determination of Molecular Structures of HIV Envelope Glycoproteins using Cryo-Electron Tomography and Automated Sub-tomogram Averaging
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Cited by 16 •
2011
The protocol describes a high-throughput approach to determining structures of membrane proteins using cryo-electron tomography and 3D image processing. It covers the details of specimen preparation, data collection, data processing and interpretation, and concludes with the production of a representative target for the approach, the HIV-1 Envelope glycoprotein. These computational procedures are designed in a way that enables researchers and students to work remotely and contribute to data...
07:10
Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay
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Cited by 44 •
2014
Understanding viral surface antigens conformations is required to evaluate antibody neutralization and guide the design of effective vaccine immunogens. Here we describe a cell-based ELISA assay that allows the study of the recognition of trimeric HIV-1 Env expressed at the surface of transfected cells by specific anti-Env antibodies.
11:45
Imaging of HIV-1 Envelope-induced Virological Synapse and Signaling on Synthetic Lipid Bilayers
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Cited by 4 •
2012
This article describes a method to visualize formation of an HIV-1 envelope-induced virological synapse on glass supported planar bilayers by total internal reflection fluorescence (TIRF) microscopy. The method can also be combined with immunofluorescence staining to detect activation and redistribution of signaling molecules that occur during HIV-1 envelope-induced virological synapse formation.
08:29
Averaging of Viral Envelope Glycoprotein Spikes from Electron Cryotomography Reconstructions using Jsubtomo
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Cited by 23 •
2014
An approach is presented for determining structures of viral membrane glycoprotein complexes using a combination of electron cryo-tomography and sub-tomogram averaging with the computational package Jsubtomo.
13:58
Amplifying and Quantifying HIV-1 RNA in HIV Infected Individuals with Viral Loads Below the Limit of Detection by Standard Clinical Assays
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Cited by 10 •
2011
Quantifying levels of HIV-1 RNA in plasma and sequencing single HIV-1 genomes from individuals with viral loads below the limit of detection (50-75 copies/ml) is difficult. Here we describe how to extract and quantify plasma viral RNA using a real time PCR assay that reliably measures HIV-1 RNA down to 0.3 copies/ml and how to amplify viral genomes by single genome sequencing, from samples with very low viral loads.
FAQs
Entry proceeds through a coordinated sequence rather than through gp120 or gp41 acting independently. First, gp120 engages CD4 and then a coreceptor, either CCR5 or CXCR4. These receptor interactions trigger structural changes in gp41, enabling it to drive fusion of viral and cellular membranes. This sequence links receptor recognition directly to membrane merger and productive entry.
Coreceptor preference helps determine which cellular entry route the virus can exploit. Envelope interactions with CCR5 or CXCR4 therefore provide a molecular basis for analyzing viral tropism, the pattern of susceptible cellular targets. Tracking this preference is relevant to infection research because entry behavior can be considered alongside transmission and disease progression.
HIV-1 envelope glycoproteins evade antibody recognition through two complementary features: extensive sequence variability and glycan shielding. Variable surfaces can alter antibody-accessible features, while glycans can mask underlying protein regions. At the same time, functional constraints preserve some areas needed for entry. This tension helps explain substantial immune escape while leaving conserved sites available as broadly neutralizing antibody targets.
Conserved functional regions are valuable because they are shared across more variable envelope forms and remain linked to essential entry activity. Broadly neutralizing antibodies can therefore target features beyond strain-specific surfaces. Studying these antibody targets informs vaccine design by identifying envelope elements that may support wider neutralization coverage despite the virus’s extensive variability.
Because the envelope complex controls receptor engagement, coreceptor use, and membrane fusion, each stage provides a mechanistic point for investigating inhibition. Researchers can examine how candidate entry inhibitors affect these interactions or fusion-related changes. Such studies connect molecular behavior with host-cell entry and help distinguish whether an intervention acts before receptor binding, during coreceptor engagement, or at fusion.
Envelope-focused analyses can connect molecular variation with several infection-related outcomes, including viral tropism, transmission, immune escape, and disease progression. They also clarify how antibody recognition relates to changing viral surfaces and conserved functional regions. In immunology and infection research, this makes the envelope useful for integrating entry mechanisms with host immune pressure and evaluating vaccine-oriented hypotheses.