Evidence map›Paper›PMID 21613393›Full record

ArticleJournal of virology2011

A tyrosine-sulfated CCR5-mimetic peptide promotes conformational transitions in the HIV-1 envelope glycoprotein.

Jo Ann Kwong, Tatyana Dorfman, Brian D Quinlan, Jessica J Chiang, Asim A Ahmed, Hyeryun Choe, Michael Farzan

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

17 citing papers in PubMed, 22 citations in OpenAlex.

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  9. Targeting strategies for delivery of anti-HIV drugs.Journal of controlled release : official journal of the Controlled Release Society · 2014
    Review
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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

7 authors at 1 institution in 1 country.

Jo Ann KwongDepartment of Pediatrics, Harvard Medical School, Children's Hospital, Boston, Massachusetts 02115, USA.
Tatyana Dorfman
Brian D Quinlan
Jessica J Chiang
Asim A Ahmed
Hyeryun Choe
Michael Farzan
Harvard University · US

Funding

ZETA CHAIN OF T CELL RECEPTOR INTERACTS W/ NEF OF SIV &HIV2P51RR000168 · NCRR · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WESTMORELAND, SUSAN V. · 1985 to 2011
$139.3M
Viral escape from AAV expressed transgenesP01AI100263 · NIAID · SCRIPPS FLORIDA · PI GAO, GUANGPING · 2012 to 2016
$11.9M
Therapeutic use of an enhanced form of CD4-IgR01AI091476 · NIAID · SCRIPPS FLORIDA · PI FARZAN, MICHAEL R. · 2011 to 2015
$4.3M
ASSOCIATION OF HIV1 GP120 WITH ITS CORECEPTORSR01AI043891 · NIAID · CHILDREN'S HOSPITAL BOSTON · PI CHOE, HYERYUN · 1999 to 2007
$2.3M
A double-mimetic inhibitor of HIV-1 entryR01AI080324 · NIAID · SCRIPPS FLORIDA · PI FARZAN, MICHAEL R. · 2009 to 2013
$2.3M
MOUSE MODELS OF CANCER, BONE DISEASE, AND LACTATIONK26RR000168 · NCRR · OHIO STATE UNIVERSITY · PI ROSOL, THOMAS J · 2000 to 2004
$547k
NCRR NIH HHS K26 RR000168NCRR NIH HHS P51 RR000168NCRR NIH HHS RR000168NIAID NIH HHS AI080324NIAID NIH HHS P01 AI100263NIAID NIH HHS R01 AI043891NIAID NIH HHS R01 AI080324NIAID NIH HHS R01 AI091476
6 · The paper itself

Abstract

The HIV-1 envelope glycoprotein is a trimeric complex of heterodimers composed of a surface glycoprotein, gp120, and a transmembrane component, gp41. The association of this complex with CD4 stabilizes the coreceptor-binding site of gp120 and promotes the exposure of the gp41 helical region 1 (HR1). Here, we show that a 15-amino-acid peptide mimetic of the HIV-1 coreceptor CCR5 fused to a dimeric antibody Fc domain (CCR5mim-Ig) bound two gp120 molecules per envelope glycoprotein complex and by itself promoted HR1 exposure. CCR5mim-Ig also stabilized the association of a CD4-mimetic peptide with the envelope glycoprotein. A fusion of the CD4- and CCR5-mimetic peptides, DM1, bound gp120 and neutralized R5, R5X4, and X4 HIV-1 isolates comparably to CD4, and they did so markedly more efficiently than either peptide alone. Our data indicate that the potency of DM1-Ig derives from its avidity for the HIV-1 envelope glycoprotein trimer and from the bidirectional induction of its receptor-mimetic components. DM1 has significant advantages over other inhibitors that target both coreceptor and CD4-binding sites, and it may serve as a lead for a new class of HIV-1 inhibitor peptides.

Indexed as

Molecular MimicryCell LineFlow CytometryHIV-1HIV Envelope Protein gp120HIV Envelope Protein gp41HumansModels, MolecularProtein ConformationReceptors, CCR5SulfatesTyrosineHIV Envelope Protein gp120HIV Envelope Protein gp41Receptors, CCR5SulfatesTyrosine

Identifiers

PMID21613393
PMCPMC3147930
OpenAlexW2130248950

What OpenQuestion holds

Textmetadata
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.