Evidence map›Paper›PMID 28209172›Full record

ArticleVirology journal2017

Evaluation of the contribution of the transmembrane region to the ectodomain conformation of the human immunodeficiency virus (HIV-1) envelope glycoprotein.

Hanh T Nguyen, Navid Madani, Haitao Ding, Emerald Elder, Amy Princiotto, Christopher Gu, Patrice Darby, James Alin, Alon Herschhorn, John C Kappes and 2 more

Open access · goldAbstract read
In one paragraph

Article in Virology journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.1field-weighted citation impact, top 26% 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

10 citing papers in PubMed, 12 citations in OpenAlex.

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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

12 authors at 4 institutions in 1 country.

Hanh T NguyenDepartment of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, 450 Brookline Avenue, CLS 1010, Boston, MA, 02215, USA.
Navid MadaniDepartment of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, 450 Brookline Avenue, CLS 1010, Boston, MA, 02215, USA.
Haitao DingDepartment of Medicine, University of Alabama at Birmingham, Birmingham, AL, 35294, USA.
Emerald ElderDepartment of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, 450 Brookline Avenue, CLS 1010, Boston, MA, 02215, USA.
Amy PrinciottoDepartment of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, 450 Brookline Avenue, CLS 1010, Boston, MA, 02215, USA.
Christopher GuDepartment of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, 450 Brookline Avenue, CLS 1010, Boston, MA, 02215, USA.
Patrice DarbyDepartment of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, 450 Brookline Avenue, CLS 1010, Boston, MA, 02215, USA.
James AlinDepartment of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, 450 Brookline Avenue, CLS 1010, Boston, MA, 02215, USA.
Alon HerschhornDepartment of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, 450 Brookline Avenue, CLS 1010, Boston, MA, 02215, USA.
John C KappesDepartment of Medicine, University of Alabama at Birmingham, Birmingham, AL, 35294, USA.
Youdong MaoDepartment of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, 450 Brookline Avenue, CLS 1010, Boston, MA, 02215, USA.
Joseph G SodroskiDepartment of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, 450 Brookline Avenue, CLS 1010, Boston, MA, 02215, USA. joseph_sodroski@dfci.harvard.edu.
Harvard University · USDana-Farber Cancer Institute · USBirmingham VA Medical Center · USUniversity of Alabama at Birmingham · US

Funding

Virus biology scientific research support componentUM1AI100645 · NIAID · DUKE UNIVERSITY · PI MCMICHAEL, ANDREW JAMES · 2012 to 2018
$204.7M
Understanding Envelope Function in HIV-1 Infection: The Design, Synthesis and Validation of Small Molecule HIV-1 Env InhibitorsP01GM056550 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI ABRAMS, CAMERON F · 1997 to 2018
$31.2M
Conformational Landscape of the HIV-1 Envelope GlycoproteinsR01AI124982 · NIAID · DANA-FARBER CANCER INST · PI SODROSKI, JOSEPH G · 2016 to 2025
$6.7M
NIAID NIH HHS R01 AI124982NIAID NIH HHS UM1 AI100645NIGMS NIH HHS P01 GM056550
6 · The paper itself

Abstract

backgroundThe human immunodeficiency virus (HIV-1) envelope glycoprotein (Env), a Type 1 transmembrane protein, assembles into a trimeric spike complex that mediates virus entry into host cells. The high potential energy of the metastable, unliganded Env trimer is maintained by multiple non-covalent contacts among the gp120 exterior and gp41 transmembrane Env subunits. Structural studies suggest that the gp41 transmembrane region forms a left-handed coiled coil that contributes to the Env trimer interprotomer contacts. Here we evaluate the contribution of the gp41 transmembrane region to the folding and stability of Env trimers.

methodsMultiple polar/charged amino acid residues, which hypothetically disrupt the stop-transfer signal, were introduced in the proposed lipid-interactive face of the transmembrane coiled coil, allowing release of soluble cleavage-negative Envs containing the modified transmembrane region (TM

resultsThe introduction of polar/charged amino acids into the transmembrane region resulted in the secretion of soluble Envs from the cell. However, these TM

conclusionThe modified transmembrane region was not conducive to trimerization of soluble Envs. However, for HIV-1 Env ectodomains that are minimally modified, membrane-anchored Envs exhibit the most native structures and can be stabilized by appropriately positioned FT domains.

Indexed as

Protein FoldingProtein MultimerizationAmino Acid SubstitutionHIV Envelope Protein gp120HIV Envelope Protein gp41HumansMutant ProteinsProtein Conformationgp120 protein, Human immunodeficiency virus 1gp41 protein, Human immunodeficiency virus 1HIV Envelope Protein gp120HIV Envelope Protein gp41Mutant ProteinsEctodomainFibritin –Trimergp41HIV-1 EnvStabilizeTransmembrane region

Identifiers

PMID28209172
PMCPMC5314615
OpenAlexW2588769814

What OpenQuestion holds

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LicenceCC BY
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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.