Evidence map›Paper›PMID 20166740›Full record

ArticleBiochemistry2010

Direct interaction of the mouse cytomegalovirus m152/gp40 immunoevasin with RAE-1 isoforms.

Li Zhi, Janet Mans, Michael J Paskow, Patrick H Brown, Peter Schuck, Stipan Jonjić, Kannan Natarajan, David H Margulies

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

22 citing papers in PubMed, 34 citations in OpenAlex.

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  16. B7-H6/NKp30 interaction: a mechanism of alerting NK cells against tumors.Cellular and molecular life sciences : CMLS · 2011
    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

8 authors at 3 institutions in 3 countries.

Li ZhiMolecular Biology Section, Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892-1892, USA.
Janet Mans
Michael J Paskow
Patrick H Brown
Peter Schuck
Stipan Jonjić
Kannan Natarajan
David H Margulies
National Institute of Allergy and Infectious Diseases · USNational Institute of Biomedical Imaging and Bioengineering · USUniversity of Rijeka · HR

Funding

Molecular Genetic Analysis Of Lymphocyte FunctionZIAAI000394 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI MARGULIES, DAVID · 2009 to 2025
$11.5M
Structure and Function of Viral ImmunoevasinsZIAAI001028 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI MARGULIES, DAVID · 2009 to 2025
$7.9M
Dynamics of Protein Assemblies by Analytical UltracentrifugationZIAEB000051 · NIBIB · NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING · PI SCHUCK, PETER · 2009 to 2025
$7.9M
Biophysical Characterization Of MacromoleculesZICEB000008 · NIBIB · NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING · PI SCHUCK, PETER · 2010 to 2010
$427k
Viral evasion of NK cellsR01AI083201 · NIAID · UNIVERSITY OF RIJEKA--MEDICAL FACULTY · PI JONJIC, STIPAN · 2009 to 2012
$331k
Dynamics of Protein Assemblies by Analytical UltracentrifugationZ01EB000051 · NIBIB · NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING · PI SCHUCK, PETER · 2007 to 2008
$111k
Intramural NIH HHS Z01 EB000051Intramural NIH HHS ZIA AI001028NIAID NIH HHS R01 AI083201
6 · The paper itself

Abstract

Cytomegaloviruses (CMVs) are ubiquitous species-specific viruses that establish acute, persistent, and latent infections. Both human and mouse CMVs encode proteins that inhibit the activation of natural killer (NK) cells by downregulating cellular ligands for the NK cell activating receptor, NKG2D. The MCMV glycoprotein m152/gp40 downregulates the surface expression of RAE-1 to prevent NK cell control in vivo. So far, it is unclear if there is a direct interaction between m152 and RAE-1 and, if so, if m152 interacts differentially with the five identified RAE-1 isoforms, which are expressed as two groups in MCMV-susceptible or -resistant mouse strains. To address these questions, we expressed and purified the extracellular domains of RAE-1 and m152 and performed size exclusion chromatography binding assays as well as analytical ultracentrifugation and isothermal titration calorimetry to characterize these interactions quantitatively. We further evaluated the role of full-length and naturally glycosylated m152 and RAE-1 in cotransfected HEK293T cells. Our results confirmed that m152 binds RAE-1 directly, relatively tightly (K(d) < 5 microM), and with 1:1 stoichiometry. The binding is quantitatively different depending on particular RAE-1 isoforms, corresponding to the susceptibility to downregulation by m152. A PLWY motif found in RAE-1beta, although contributing to its affinity for m152, does not influence the affinity of RAE-1gamma or RAE-1delta, suggesting that other differences contribute to the RAE-1-m152 interaction. Molecular modeling of the different RAE-1 isoforms suggests a potential site for the m152 interaction.

Indexed as

MuromegalovirusAmino Acid MotifsAmino Acid SequenceAnimalsBinding, CompetitiveCell LineDown-RegulationHumansMembrane GlycoproteinsMembrane ProteinsMiceModels, MolecularMolecular Sequence DataNK Cell Lectin-Like Receptor Subfamily KProtein BindingProtein Conformationm152 protein, cytomegalovirusMembrane GlycoproteinsMembrane ProteinsNK Cell Lectin-Like Receptor Subfamily KProtein IsoformsViral Proteins

Identifiers

PMID20166740
PMCPMC2840211
OpenAlexW1975613049

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.