Evidence map›Paper›PMID 29561264›Full record

ArticleeLife2018

HIV-1 Env trimer opens through an asymmetric intermediate in which individual protomers adopt distinct conformations.

Xiaochu Ma, Maolin Lu, Jason Gorman, Daniel S Terry, Xinyu Hong, Zhou Zhou, Hong Zhao, Roger B Altman, James Arthos, Scott C Blanchard and 3 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 120 papers.

0numbers the graph read from it
0cells of the map it votes in
120citing papers in PubMed
10.4field-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

120 citing papers in PubMed, 164 citations in OpenAlex.

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60 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 4 institutions in 1 country.

Xiaochu MaDepartment of Microbial Pathogenesis, Yale University School of Medicine, New Haven, United States.
Maolin LuDepartment of Microbial Pathogenesis, Yale University School of Medicine, New Haven, United States.
Jason GormanVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, United States.
Daniel S TerryDepartment of Physiology and Biophysics, Weill Cornell Medical College of Cornell University, New York, United States.
Xinyu HongDepartment of Microbial Pathogenesis, Yale University School of Medicine, New Haven, United States.
Zhou ZhouDepartment of Physiology and Biophysics, Weill Cornell Medical College of Cornell University, New York, United States.
Hong ZhaoDepartment of Physiology and Biophysics, Weill Cornell Medical College of Cornell University, New York, United States.
Roger B AltmanDepartment of Physiology and Biophysics, Weill Cornell Medical College of Cornell University, New York, United States.
James ArthosLaboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, United States.
Scott C BlanchardDepartment of Physiology and Biophysics, Weill Cornell Medical College of Cornell University, New York, United States.ORCID http://orcid.org/0000-0003-2717-9365
Peter D KwongVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, United States.
James B MunroDepartment of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, United States.
Walther MothesDepartment of Microbial Pathogenesis, Yale University School of Medicine, New Haven, United States.ORCID http://orcid.org/0000-0002-3367-7240
Cornell University · USYale University · USNational Institutes of Health · USTufts University · US

Funding

Translational ScienceP30AI042853 · NIAID · MIRIAM HOSPITAL · PI LARRY K BROWN · 1998 to 2026
$51.7M
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
Mechanisms Of Humoral EvasionZIAAI005023 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI ZHOU, TONGQING · 2009 to 2025
$18.6M
TRD #3: An automated and streamlined pipeline for in-situ molecular microscopyP41GM103310 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2012 to 2021
$14.7M
Interaction of HIV envelope with cell surface receptorsZIAAI000883 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI ARTHOS, JAMES L · 2009 to 2024
$14.0M
Next-generation Fluorescent Probes for Biological ResearchR01GM098859 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI BLANCHARD, SCOTT C · 2012 to 2019
$2.9M
Single molecule imaging of HIV-1 entryR01GM116654 · NIGMS · YALE UNIVERSITY · PI MOTHES, WALTHER H · 2015 to 2018
$1.6M
Mechanisms Of Humoral EvasionZ01AI005023 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI KWONG, PETER D · 2002 to 2008
$564k
HIV-1 Env antagonism by ground state stabilizationK22AI116262 · NIAID · TUFTS UNIVERSITY BOSTON · PI MUNRO, JAMES B · 2015 to 2016
$266k
Cancer Research Institute Irvington Fellows ProgramIntramural NIH HHS Z01 AI005023NIAID NIH HHS K22 AI116262NIAID NIH HHS P30 AI042853NIGMS NIH HHS P01 GM056550NIGMS NIH HHS P41 GM103310NIGMS NIH HHS R01 GM098859NIGMS NIH HHS R01 GM116654NIH HHS AI005023-17NIH HHS AI042853NIH HHS AI116262NIH HHS GM056550NIH HHS GM098859NIH HHS GM103310NIH HHS GM116654
6 · The paper itself

Abstract

HIV-1 entry into cells requires binding of the viral envelope glycoprotein (Env) to receptor CD4 and coreceptor. Imaging of individual Env molecules on native virions shows Env trimers to be dynamic, spontaneously transitioning between three distinct well-populated conformational states: a pre-triggered Env (State 1), a default intermediate (State 2) and a three-CD4-bound conformation (State 3), which can be stabilized by binding of CD4 and coreceptor-surrogate antibody 17b. Here, using single-molecule Fluorescence Resonance Energy Transfer (smFRET), we show the default intermediate configuration to be asymmetric, with individual protomers adopting distinct conformations. During entry, this asymmetric intermediate forms when a single CD4 molecule engages the trimer. The trimer can then transition to State 3 by binding additional CD4 molecules and coreceptor.

Indexed as

Protein ConformationProtein MultimerizationCD4 Antigensenv Gene Products, Human Immunodeficiency VirusFluorescence Resonance Energy TransferHIV-1HIV AntibodiesHIV Envelope Protein gp120HumansProtein BindingProtein SubunitsVirionCD4 Antigensenv Gene Products, Human Immunodeficiency VirusHIV AntibodiesHIV Envelope Protein gp120Protein SubunitsHIV-1 Envelopeinfectious diseasemicrobiologymolecular biophysicsSingle molecule FRETstructural biologyvirusvirus entry

Identifiers

PMID29561264
PMCPMC5896952
OpenAlexW2792975318

What OpenQuestion holds

Textmetadata
LicenceCC0
Read underepoch 390

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.