Evidence map›Paper›PMID 26113642›Full record

ArticleScience (New York, N.Y.)2015

HIV-1 ENVELOPE. Effect of the cytoplasmic domain on antigenic characteristics of HIV-1 envelope glycoprotein.

Jia Chen, James M Kovacs, Hanqin Peng, Sophia Rits-Volloch, Jianming Lu, Donghyun Park, Elise Zablowsky, Michael S Seaman, Bing Chen

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing 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

99 citing papers in PubMed.

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Jia ChenDivision of Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA. Department of Pediatrics, Harvard Medical School, 3 Blackfan Street, Boston, MA 02115, USA.
James M KovacsDivision of Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA. Department of Pediatrics, Harvard Medical School, 3 Blackfan Street, Boston, MA 02115, USA.
Hanqin PengDivision of Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA.
Sophia Rits-VollochDivision of Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA.
Jianming LuCodex BioSolutions, Inc., 401 Professional Drive, Gaithersburg, MD 20879, USA.
Donghyun ParkDivision of Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA.
Elise ZablowskyCenter for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, 330 Brookline Avenue, Boston, MA 02215, USA.
Michael S SeamanCenter for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, 330 Brookline Avenue, Boston, MA 02215, USA.
Bing ChenDivision of Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA. Department of Pediatrics, Harvard Medical School, 3 Blackfan Street, Boston, MA 02115, USA. bchen@crystal.harvard.edu.

Funding

Virus biology scientific research support componentUM1AI100645 · NIAID · DUKE UNIVERSITY · PI MCMICHAEL, ANDREW JAMES · 2012 to 2018
$204.7M
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
NIAID NIH HHS AI084794NIAID NIH HHS AI-100645NIAID NIH HHS AI106488NIAID NIH HHS R01 AI084794NIAID NIH HHS R01 AI106488NIAID NIH HHS UM1 AI100645NIGMS NIH HHS GM083680NIGMS NIH HHS R01 GM083680
6 · The paper itself

Abstract

A major goal for HIV-1 vaccine development is the production of an immunogen to mimic native, functional HIV-1 envelope trimeric spikes (Env) on the virion surface. We lack a reliable description of a native, functional trimer, however, because of inherent instability and heterogeneity in most preparations. We describe here two conformationally homogeneous Envs derived from difficult-to-neutralize primary isolates. All their non-neutralizing epitopes are fully concealed and independent of their proteolytic processing. Most broadly neutralizing antibodies (bnAbs) recognize these native trimers. Truncation of their cytoplasmic tail has little effect on membrane fusion, but it diminishes binding to trimer-specific bnAbs while exposing non-neutralizing epitopes. These results yield a more accurate antigenic picture than hitherto possible of a genuinely untriggered and functional HIV-1 Env; they can guide effective vaccine development.

Indexed as

AIDS VaccinesAntibodies, NeutralizingAntigensCD4 AntigensCytoplasmEpitopesHIV-1HIV AntibodiesHIV Envelope Protein gp120HIV Envelope Protein gp160HIV Envelope Protein gp41HIV InfectionsHumansProtein Structure, TertiaryVirionAIDS VaccinesAntibodies, NeutralizingAntigensCD4 AntigensEpitopesgp120 protein, Human immunodeficiency virus 1gp160 protein, Human immunodeficiency virus 1gp41 protein, Human immunodeficiency virus 1HIV AntibodiesHIV Envelope Protein gp120HIV Envelope Protein gp160HIV Envelope Protein gp41

Identifiers

PMID26113642
PMCPMC4701381

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.