Evidence map›Paper›PMID 19833723›Full record

ArticleThe Journal of biological chemistry2010

HIV-1 transmission by dendritic cell-specific ICAM-3-grabbing nonintegrin (DC-SIGN) is regulated by determinants in the carbohydrate recognition domain that are absent in liver/lymph node-SIGN (L-SIGN).

Nancy P Y Chung, Sabine K J Breun, Arman Bashirova, Joerg G Baumann, Thomas D Martin, Jaideep M Karamchandani, Jason W Rausch, Stuart F J Le Grice, Li Wu, Mary Carrington and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. 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
0.8field-weighted citation impact, top 31% 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, 31 citations in OpenAlex.

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  7. HIV-1 envelope proteins up-regulateThe Journal of biological chemistry · 2019
    Article
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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

11 authors at 5 institutions in 2 countries.

Nancy P Y ChungHIV Drug Resistance Program, NCI-Frederick, National Institutes of Health, Frederick, Maryland 21702, USA.
Sabine K J Breun
Arman Bashirova
Joerg G Baumann
Thomas D Martin
Jaideep M Karamchandani
Jason W Rausch
Stuart F J Le Grice
Li Wu
Mary Carrington
Vineet N Kewalramani
Frederick National Laboratory for Cancer Research · USFraunhofer Institute for Cell Therapy and Immunology · DENational Institutes of Health · USScience Applications International Corporation (United States) · USMedical College of Wisconsin · US

Funding

Effects of genetic polymorphism in MHC, KIR, and related loci on human diseaseZIABC010791 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI CARRINGTON, MARY N. · 2009 to 2025
$18.2M
Viral and Host Proteins as Therapeutic TargetsZIABC010494 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI LE GRICE, STUART F. J. · 2009 to 2021
$9.0M
Mechanism of DC-SIGN-Mediated Transmission of HIVZIABC010485 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI KEWALRAMANI, VINEET N · 2009 to 2011
$499k
CCR NIH HHS HHSN261200800001CIntramural NIH HHS ZIA BC010494NCI NIH HHS HHSN261200800001E
6 · The paper itself

Abstract

In this study, we identify determinants in dendritic cell-specific ICAM-3-grabbing nonintegrin (DC-SIGN) necessary for human immunodeficiency virus, type 1 (HIV-1), transmission. Although human B cell lines expressing DC-SIGN efficiently capture and transmit HIV-1 to susceptible target cells, cells expressing the related molecule liver/lymph node-specific ICAM-3-grabbing nonintegrin (L-SIGN) do not. To understand the differences between DC-SIGN and L-SIGN that affect HIV-1 interactions, we developed Raji B cell lines expressing different DC-SIGN/L-SIGN chimeras. Testing of the chimeras demonstrated that replacement of the DC-SIGN carbohydrate-recognition domain (CRD) with that of L-SIGN was sufficient to impair virus binding and prevent transmission. Conversely, the ability to bind and transmit HIV-1 was conferred to L-SIGN chimeras containing the DC-SIGN CRD. We identified Trp-258 in the DC-SIGN CRD to be essential for HIV-1 transmission. Although introduction of a K270W mutation at the same position in L-SIGN was insufficient for HIV-1 binding, an L-SIGN mutant molecule with K270W and a C-terminal DC-SIGN CRD subdomain transmitted HIV-1. These data suggest that DC-SIGN structural elements distinct from the oligosaccharide-binding site are required for HIV-1 glycoprotein selectivity.

Indexed as

Carbohydrate MetabolismHIV-1AllelesAnimalsB-LymphocytesCell Adhesion MoleculesCell LineDC-Specific ICAM-3 Grabbing NonintegrinGene Expression RegulationHIV InfectionsHumansLectinsLectins, C-TypeMiceModels, MolecularProtein Structure, TertiaryCell Adhesion MoleculesCLEC4M protein, humanDC-Specific ICAM-3 Grabbing NonintegrinLectinsLectins, C-TypeReceptors, Cell SurfaceRecombinant Fusion Proteins

Identifiers

PMID19833723
PMCPMC2804366
OpenAlexW2068221826

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.