Evidence map›Paper›PMID 17006538›Full record

ArticleThe EMBO journal2006

Restraining the conformation of HIV-1 gp120 by removing a flexible loop.

Sophia Rits-Volloch, Gary Frey, Stephen C Harrison, Bing Chen

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.9field-weighted citation impact, top 30% 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

14 citing papers in PubMed, 24 citations in OpenAlex.

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  13. A fusion-intermediate state of HIV-1 gp41 targeted by broadly neutralizing antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2008
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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

4 authors at 3 institutions in 1 country.

Sophia Rits-VollochLaboratory of Molecular Medicine, The Children's Hospital, Boston, MA 02115, USA.
Gary Frey
Stephen C Harrison
Bing Chen
Howard Hughes Medical Institute · USBoston Children's Hospital · USHarvard University · US

Funding

Viral Sequencing CoreU19AI067854 · NIAID · DUKE UNIVERSITY · PI LETVIN, NORMAN L · 2006 to 2011
$290.5M
Viral and Host Determinants of HIV-1 TransmissionU01AI067854 · NIAID · DUKE UNIVERSITY · PI HARRISON, STEPHEN COPLAN · 2005 to 2005
$14.9M
Structures of HIV and SIV envelope glycoproteinsR01GM075752 · NIGMS · CHILDREN'S HOSPITAL BOSTON · PI HARRISON, STEPHEN COPLAN · 2005 to 2008
$781k
NIAID NIH HHS AI-67854NIAID NIH HHS U01 AI067854NIAID NIH HHS U19 AI067854NIGMS NIH HHS GM-75752NIGMS NIH HHS R01 GM075752
6 · The paper itself

Abstract

The trimeric HIV/SIV envelope glycoprotein, gp160, is cleaved to noncovalently associated fragments, gp120 and gp41. Binding of gp120 to viral receptors leads to large structural rearrangements in both fragments. The unliganded gp120 core has a disordered beta3-beta5 loop, which reconfigures upon CD4 binding into an ordered, extended strand. Molecular modeling suggests that residues in this loop may contact gp41. We show here that deletions in the beta3-beta5 loop of HIV-1 gp120 weaken the binding of CD4 and prevent formation of the epitope for monoclonal antibody (mAb) 17b (which recognizes the coreceptor site). Formation of an encounter complex with CD4 binding and interactions of gp120 with mAbs b12 and 2G12 are not affected by these deletions. Thus, deleting the beta3-beta5 loop blocks the gp120 conformational change and may offer a strategy for design of restrained immunogens. Moreover, mutations in the SIV beta3-beta5 loop lead to greater spontaneous dissociation of gp120 from cell-associated trimers. We suggest that the CD4-induced rearrangement of this loop releases structural constraints on gp41 and thus potentiates its fusion activity.

Indexed as

Models, MolecularAntibodies, MonoclonalCD4 AntigensGene Products, envHIV-1HIV Envelope Protein gp120HIV Envelope Protein gp41HumansMultiprotein ComplexesProtein BindingProtein Structure, QuaternaryProtein Structure, SecondaryStructure-Activity RelationshipAntibodies, MonoclonalCD4 AntigensGene Products, envHIV Envelope Protein gp120HIV Envelope Protein gp41Multiprotein ComplexesSIV envelope glycoprotein gp160

Identifiers

PMID17006538
PMCPMC1618118
OpenAlexW2140283479

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.