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Trimerization of the HIV Transmembrane Domain in Lipid Bilayers Modulates Broadly Neutralizing Antibody Binding

https://doi.org/10.1002/anie.201508421

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Peptides as transmembrane segments: Decrypting the determinants for helix–helix interactions in membrane proteins

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Universal Sensing by Transduction of Antibody Binding with Backscattering Interferometry

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Membrane protein assembly into Nanodiscs

inferredcites →https://doi.org/10.1016/s0076-6879(09)64011-8openalex-snapshot

Reconstitution of Membrane Proteins in Phospholipid Bilayer Nanodiscs

inferredcites →https://doi.org/10.1021/bi501376fopenalex-snapshot

Conditional Trimerization and Lytic Activity of HIV-1 gp41 Variants Containing the Membrane-Associated Segments

inferredcites →https://doi.org/10.1021/bi802303bopenalex-snapshot

Structure of the HIV-1 gp41 Membrane-Proximal Ectodomain Region in a Putative Prefusion Conformation,

inferredcites →https://doi.org/10.1021/ja0393574openalex-snapshot

Directed Self-Assembly of Monodisperse Phospholipid Bilayer Nanodiscs with Controlled Size

inferredcites →https://doi.org/10.1021/ja047820mopenalex-snapshot

Label-Free Molecular Interaction Determinations with Nanoscale Interferometry

inferredcites →https://doi.org/10.1021/nl025623kopenalex-snapshot

Self-Assembly of Discoidal Phospholipid Bilayer Nanoparticles with Membrane Scaffold Proteins

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Distribution and three-dimensional structure of AIDS virus envelope spikes

inferredcites →https://doi.org/10.1038/nature07159openalex-snapshot

Molecular architecture of native HIV-1 gp120 trimers

inferredcites →https://doi.org/10.1038/nature11544openalex-snapshot

Broad and potent neutralization of HIV-1 by a gp41-specific human antibody

inferredcites →https://doi.org/10.1038/nbt.1790openalex-snapshot

Label-free quantification of membrane-ligand interactions using backscattering interferometry

inferredcites →https://doi.org/10.1038/nsmb.2351openalex-snapshot

Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer

inferredcites →https://doi.org/10.1073/pnas.0800255105openalex-snapshot

A fusion-intermediate state of HIV-1 gp41 targeted by broadly neutralizing antibodies

inferredcites →https://doi.org/10.1073/pnas.0901474106openalex-snapshot

Broadly neutralizing anti-HIV-1 antibodies disrupt a hinge-related function of gp41 at the membrane interface

inferredcites →https://doi.org/10.1073/pnas.0908713106openalex-snapshot

Role of HIV membrane in neutralization by two broadly neutralizing antibodies

inferredcites →https://doi.org/10.1073/pnas.0909680107openalex-snapshot

Aromatic residues at the edge of the antibody combining site facilitate viral glycoprotein recognition through membrane interactions

inferredcites →https://doi.org/10.1073/pnas.1007227107openalex-snapshot

Single-particle cryoelectron microscopy analysis reveals the HIV-1 spike as a tripod structure

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Scaffolding to build a rational vaccine design strategy

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Trimeric HIV-1 glycoprotein gp140 immunogens and native HIV-1 envelope glycoproteins display the same closed and open quaternary molecular architectures

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Limited or no protection by weakly or nonneutralizing antibodies against vaginal SHIV challenge of macaques compared with a strongly neutralizing antibody

inferredcites →https://doi.org/10.1073/pnas.1415789111openalex-snapshot

Recombinant HIV envelope trimer selects for quaternary-dependent antibodies targeting the trimer apex

inferredcites →https://doi.org/10.1073/pnas.201392898openalex-snapshot

Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region

inferredcites →https://doi.org/10.1073/pnas.98.3.880openalex-snapshot

Polar side chains drive the association of model transmembrane peptides

inferredcites →https://doi.org/10.1074/jbc.m113.527747openalex-snapshot

Structure and Immunogenicity of a Peptide Vaccine, Including the Complete HIV-1 gp41 2F5 Epitope

inferredcites →https://doi.org/10.1084/jem.20101907openalex-snapshot

MPER-specific antibodies induce gp120 shedding and irreversibly neutralize HIV-1

inferredcites →https://doi.org/10.1089/aid.2008.0213openalex-snapshot

Oligomer-Specific Conformations of the Human Immunodeficiency Virus (HIV-1) gp41 Envelope Glycoprotein Ectodomain Recognized by Human Monoclonal Antibodies

inferredcites →https://doi.org/10.1126/science.1057453openalex-snapshot

Protein Design of an HIV-1 Entry Inhibitor

inferredcites →https://doi.org/10.1126/science.1213256openalex-snapshot

A Potent and Broad Neutralizing Antibody Recognizes and Penetrates the HIV Glycan Shield

inferredcites →https://doi.org/10.1126/science.1245625openalex-snapshot

Crystal Structure of a Soluble Cleaved HIV-1 Envelope Trimer

inferredcites →https://doi.org/10.1126/science.1245627openalex-snapshot

Cryo-EM Structure of a Fully Glycosylated Soluble Cleaved HIV-1 Envelope Trimer

inferredcites →https://doi.org/10.1126/science.aac7800openalex-snapshot

The modern era of HIV-1 vaccine development

inferredcites →https://doi.org/10.1126/scitranslmed.3008992openalex-snapshot

Neutralizing antibodies to HIV-1 envelope protect more effectively in vivo than those to the CD4 receptor

inferredcites →https://doi.org/10.1128/jvi.00756-11openalex-snapshot

Direct Antibody Access to the HIV-1 Membrane-Proximal External Region Positively Correlates with Neutralization Sensitivity

inferredcites →https://doi.org/10.1128/jvi.02257-09openalex-snapshot

Relationship between Antibody 2F5 Neutralization of HIV-1 and Hydrophobicity of Its Heavy Chain Third Complementarity-Determining Region

inferredcites →https://doi.org/10.1128/jvi.02588-06openalex-snapshot

An Affinity-Enhanced Neutralizing Antibody against the Membrane-Proximal External Region of Human Immunodeficiency Virus Type 1 gp41 Recognizes an Epitope between Those of 2F5 and 4E10

inferredcites →https://doi.org/10.1128/jvi.06349-11openalex-snapshot

Neutralizing Epitopes in the Membrane-Proximal External Region of HIV-1 gp41 Are Influenced by the Transmembrane Domain and the Plasma Membrane

inferredcites →https://doi.org/10.1128/jvi.75.22.10892-10905.2001openalex-snapshot

Broadly Neutralizing Antibodies Targeted to the Membrane-Proximal External Region of Human Immunodeficiency Virus Type 1 Glycoprotein gp41

inferredcites →https://doi.org/10.1128/jvi.76.15.7863-7867.2002openalex-snapshot

Oligomeric Structure of the Human Immunodeficiency Virus Type 1 Envelope Protein on the Virion Surface

inferredcites →https://doi.org/10.1128/jvi.78.19.10724-10737.2004openalex-snapshot

Structure and Mechanistic Analysis of the Anti-Human Immunodeficiency Virus Type 1 Antibody 2F5 in Complex with Its gp41 Epitope

inferredcites →https://doi.org/10.1128/mmbr.00020-07openalex-snapshot

The Membrane-Proximal External Region of the Human Immunodeficiency Virus Type 1 Envelope: Dominant Site of Antibody Neutralization and Target for Vaccine Design

inferredcites →https://doi.org/10.1186/1742-4690-11-44openalex-snapshot

Anti-MPER antibodies with heterogeneous neutralization capacity are detectable in most untreated HIV-1 infected individuals

inferredcites →https://doi.org/10.1371/journal.ppat.1000880openalex-snapshot

Crystal Structure of HIV-1 gp41 Including Both Fusion Peptide and Membrane Proximal External Regions

inferredcites →https://doi.org/10.1371/journal.ppat.1004271openalex-snapshot

Antibody to gp41 MPER Alters Functional Properties of HIV-1 Env without Complete Neutralization

inferredcites →https://doi.org/10.4049/jimmunol.178.7.4424openalex-snapshot

The Role of Antibody Polyspecificity and Lipid Reactivity in Binding of Broadly Neutralizing Anti-HIV-1 Envelope Human Monoclonal Antibodies 2F5 and 4E10 to Glycoprotein 41 Membrane Proximal Envelope Epitopes

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Structural Basis for Broad HIV-1 Neutralization by a Novel MPER-Specific Human Broadly Neutralizing Antibody

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Chemical Synthesis of Membrane Proteins

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Alternatives to Detergents for Handling Membrane Proteins in Aqueous Solutions

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Exposure of the HIV-1 broadly neutralizing antibody 10E8 MPER epitope on the membrane surface by gp41 transmembrane domain scaffolds

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Advanced applications of Nanodiscs-based platforms for antibodies discovery

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HIV-1 Env gp41 Transmembrane Domain Dynamics Are Modulated by Lipid, Water, and Ion Interactions

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Structural Basis for Broad HIV-1 Neutralization by the MPER-Specific Human Broadly Neutralizing Antibody LN01

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Bionanotechnology for vaccine design

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Screening and characterization of inhibitory vNAR targeting nanodisc-assembled influenza M2 proteins

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Cloning, expression and nanodiscs assemble of recombinant HIV-1 gp41

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Nanodiscs for the study of membrane proteins

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Influence of membrane on the antigen presentation of the HIV-1 envelope membrane proximal external region (MPER)

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Review: Membrane protein nanodiscs for antibody discovery

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Nanodiscs in Membrane Biochemistry and Biophysics

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Oxidative Trimerization of Amino Acids: Selective Synthesis of 2,3,5-Trisubstituted Pyridines

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Nanoyeast and Other Cell Envelope Compositions for Protein Studies and Biosensor Applications

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Cell-Free Expression of Nipah Virus Transmembrane Proteins for Proteoliposome Vaccine Design

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Tilted, Uninterrupted, Monomeric HIV-1 gp41 Transmembrane Helix from Residual Dipolar Couplings

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Nanodiscs for structural and functional studies of membrane proteins

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Proteoliposomal formulations of an HIV-1 gp41-based miniprotein elicit a lipid-dependent immunodominant response overlapping the 2F5 binding motif

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Antigp41 membrane proximal external region antibodies and the art of using the membrane for neutralization

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Role of TMDs in Class I viral fusion proteins

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Insights into the Conformation of the Membrane Proximal Regions Critical to the Trimerization of the HIV-1 gp41 Ectodomain Bound to Dodecyl Phosphocholine Micelles

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The power, pitfalls and potential of the nanodisc system for NMR-based studies

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The Conserved Positive Charge in the Transmembrane Domain of HIV Gp41 Contributes to Its Intrinsic Preference for Trimerization

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The Interplay between HIV-1 Gag Binding to the Plasma Membrane and Env Incorporation

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Viral Membrane Fusion and the Transmembrane Domain

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Caractérisation des activités antivirales des anticorps anti-VIH-1 et anti-SARS-CoV-2

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Les IgA anti VIH-1 protecteurs comme lien entre immunité innée et adaptative : recrutement et activation des cellules effectrices par des IgA anti-gp41 pour éliminer les cellules infectées par le VIH-1 et potentielle coopération avec les IgG

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