Evidence map›Paper›PMID 27338706›Full record

ArticleScience (New York, N.Y.)2016

Structural basis for membrane anchoring of HIV-1 envelope spike.

Jyoti Dev, Donghyun Park, Qingshan Fu, Jia Chen, Heather Jiwon Ha, Fadi Ghantous, Tobias Herrmann, Weiting Chang, Zhijun Liu, Gary Frey and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed
17.8field-weighted citation impact, top 1% of its field
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

97 citing papers in PubMed, 190 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Conformational Variability of HIV-1 Env Trimer and Viral Vulnerability.bioRxiv : the preprint server for biology · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Inconspicuous Yet Indispensable: The Coronavirus Spike Transmembrane Domain.International journal of molecular sciences · 2023
    Review
  16. Article
  17. A Uniquely Stable Trimeric Model of SARS-CoV-2 Spike Transmembrane Domain.International journal of molecular sciences · 2022
    Article
  18. Article
  19. Posttranslational modifications optimize the ability of SARS-CoV-2 spike for effective interaction with host cell receptors.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  20. Review

37 more citing papers are in PubMed but not listed here.

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

13 authors at 3 institutions in 1 country.

Jyoti Dev *Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 250 Longwood Avenue, Boston, MA 02115.
Donghyun Park *Division of Molecular Medicine, Boston Children's Hospital, 3 Blackfan Street, Boston, MA 02115.
Qingshan FuDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 250 Longwood Avenue, Boston, MA 02115.
Jia ChenDivision of Molecular Medicine, Boston Children's Hospital, 3 Blackfan Street, Boston, MA 02115.
Heather Jiwon HaDivision of Molecular Medicine, Boston Children's Hospital, 3 Blackfan Street, Boston, MA 02115.
Fadi GhantousCenter for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, 330 Brookline Avenue, Boston, MA 02215.
Tobias HerrmannVirology Program, Harvard Medical School, 260 Longwood Avenue, Boston, MA 02115.
Weiting ChangDivision of Molecular Medicine, Boston Children's Hospital, 3 Blackfan Street, Boston, MA 02115.
Zhijun LiuState Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai 200031, China.
Gary FreyDivision of Molecular Medicine, Boston Children's Hospital, 3 Blackfan Street, Boston, MA 02115.
Michael S SeamanCenter for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, 330 Brookline Avenue, Boston, MA 02215.
Bing ChenDivision of Molecular Medicine, Boston Children's Hospital, 3 Blackfan Street, Boston, MA 02115.
James J ChouDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 250 Longwood Avenue, Boston, MA 02115.
Harvard University · USBoston Children's Hospital · USBeth Israel Deaconess Medical Center · US

Funding

Virus biology scientific research support componentUM1AI100645 · NIAID · DUKE UNIVERSITY · PI HAHN, BEATRICE H · 2012 to 2018
$204.7M
OverallP41EB002026 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2018
$17.9M
Structures of Alpha 4 Integrins, Ligands and AntagonistsP01HL103526 · NHLBI · IMMUNE DISEASE INSTITUTE, INC. · PI SPRINGER, TIMOTHY A · 2011 to 2015
$11.1M
Structure-function studies of the membrane-interacting domains of HIV-1 Env spikeR01AI127193 · NIAID · BOSTON CHILDREN'S HOSPITAL · PI CHEN, BING, HARRISON, STEPHEN COPLAN · 2016 to 2025
$8.4M
Impact of HIV Envelope Conformation on ImmunogenicityR01AI084794 · NIAID · BETH ISRAEL DEACONESS MEDICAL CENTER · PI BAROUCH, DAN H., CHEN, BING · 2009 to 2013
$4.0M
Crystallographic studies of intact and fully glycosylated HIV-1 gp120R01AI106488 · NIAID · BOSTON CHILDREN'S HOSPITAL · PI CHEN, BING · 2013 to 2017
$2.2M
Biochemical and structural studies of distinct conformational states of gp41R01GM083680 · NIGMS · BOSTON CHILDREN'S HOSPITAL · PI CHEN, BING · 2009 to 2013
$1.8M
NHLBI NIH HHS HL103526NHLBI NIH HHS P01 HL103526NIAID NIH HHS AI084794NIAID NIH HHS AI-100645NIAID NIH HHS AI106488NIAID NIH HHS AI127193NIAID NIH HHS R01 AI084794NIAID NIH HHS R01 AI106488NIAID NIH HHS R01 AI127193NIAID NIH HHS UM1 AI100645NIBIB NIH HHS P41 EB-002026NIBIB NIH HHS P41 EB002026NIGMS NIH HHS GM083680NIGMS NIH HHS R01 GM083680
6 · The paper itself

Abstract

HIV-1 envelope spike (Env) is a type I membrane protein that mediates viral entry. We used nuclear magnetic resonance to determine an atomic structure of the transmembrane (TM) domain of HIV-1 Env reconstituted in bicelles that mimic a lipid bilayer. The TM forms a well-ordered trimer that protects a conserved membrane-embedded arginine. An amino-terminal coiled-coil and a carboxyl-terminal hydrophilic core stabilize the trimer. Individual mutations of conserved residues did not disrupt the TM trimer and minimally affected membrane fusion and infectivity. Major changes in the hydrophilic core, however, altered the antibody sensitivity of Env. These results show how a TM domain anchors, stabilizes, and modulates a viral envelope spike and suggest that its influence on Env conformation is an important consideration for HIV-1 immunogen design.

Indexed as

Membrane FusionVirus InternalizationArginineHIV-1HIV AntibodiesHIV Envelope Protein gp41Lipid BilayersMutationNuclear Magnetic Resonance, BiomolecularProtein MultimerizationProtein StabilityProtein Structure, TertiaryArginineHIV AntibodiesHIV Envelope Protein gp41Lipid Bilayers

Identifiers

PMID27338706
PMCPMC5085267
OpenAlexW2470057990

What OpenQuestion holds

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Registered trials

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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.