Evidence map›Paper›PMID 26799917›Full record

ArticleAngewandte Chemie (International ed. in English)2016

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

Timothy M Reichart, Michael M Baksh, Jin-Kyu Rhee, Jason D Fiedler, Stephen G Sligar, M G Finn, Michael B Zwick, Philip E Dawson

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed.

  1. Article
  2. Nanodiscs for the study of membrane proteins.Current opinion in structural biology · 2024
    Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Bionanotechnology for vaccine design.Current opinion in biotechnology · 2018
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Timothy M ReichartDepartment of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA, 92037, USA.
Michael M BakshDepartment of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA, 92037, USA.
Jin-Kyu RheeDepartment of Food Science and Engineering, Ewha Womans University, Seoul, 03760, Korea.
Jason D FiedlerDepartment of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA, 92037, USA.
Stephen G SligarDepartment of Biochemistry, University of Illinois, Urbana, IL, 61801, USA.
M G FinnDepartment of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA, 92037, USA.
Michael B ZwickDepartment of Immunology and Microbial Science, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA, USA.
Philip E DawsonDepartment of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA, 92037, USA.

Funding

METALLOENZYME MECHANISMSR01GM033775 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI SLIGAR, STEPHEN G. · 1985 to 2014
$5.2M
Eliciting antibodies to probe native trimeric gp41 for HIV vaccine designR01AI114401 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI ZWICK, MICHAEL B · 2014 to 2018
$2.9M
Synthetic Protein ChemistryR01GM098871 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DAWSON, PHILIP E · 2011 to 2014
$1.4M
Structural Relay Methods for Functional Peptide DiscoveryR21EB015663 · NIBIB · SCRIPPS RESEARCH INSTITUTE, THE · PI FINN, M.G., ORDOUKHANIAN, PHILLIP TODD · 2012 to 2013
$460k
NIAID NIH HHS AI114401NIAID NIH HHS R01 AI114401NIBIB NIH HHS EB015663NIBIB NIH HHS R21 EB015663NIGMS NIH HHS GM098871NIGMS NIH HHS GM33775NIGMS NIH HHS R01 GM033775NIGMS NIH HHS R01 GM098871
6 · The paper itself

Abstract

The membrane-proximal external region (MPER) of HIV gp41 is an established target of antibodies that neutralize a broad range of HIV isolates. To evaluate the role of the transmembrane (TM) domain, synthetic MPER-derived peptides were incorporated into lipid nanoparticles using natural and designed TM domains, and antibody affinity was measured using immobilized and solution-based techniques. Peptides incorporating the native HIV TM domain exhibit significantly stronger interactions with neutralizing antibodies than peptides with a monomeric TM domain. Furthermore, a peptide with a trimeric, three-helix bundle TM domain recapitulates the binding profile of the native sequence. These studies suggest that neutralizing antibodies can bind the MPER when the TM domain is a three-helix bundle and this presentation could influence the binding of neutralizing antibodies to the virus. Lipid-bilayer presentation of viral antigens in Nanodiscs is a new platform for evaluating neutralizing antibodies.

Indexed as

Lipid BilayersAntibodies, NeutralizingBiopolymersEnzyme-Linked Immunosorbent AssayHIV Envelope Protein gp41Antibodies, NeutralizingBiopolymersHIV Envelope Protein gp41Lipid BilayersantibodiesHIVmembrane proteinsnanostructurespeptides

Identifiers

PMID26799917
PMCPMC5405556

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.