Evidence map›Paper›PMID 23169621›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Structural basis of mouse cytomegalovirus m152/gp40 interaction with RAE1γ reveals a paradigm for MHC/MHC interaction in immune evasion.

Rui Wang, Kannan Natarajan, Maria Jamela R Revilleza, Lisa F Boyd, Li Zhi, Huaying Zhao, Howard Robinson, David H Margulies

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

19 citing papers in PubMed, 32 citations in OpenAlex.

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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 4 institutions in 1 country.

Rui WangMolecular Biology Section, Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Kannan Natarajan
Maria Jamela R Revilleza
Lisa F Boyd
Li Zhi
Huaying Zhao
Howard Robinson
David H Margulies
National Institutes of Health · USNational Institute of Allergy and Infectious Diseases · USNational Institute of Biomedical Imaging and Bioengineering · USNational Synchrotron Light Source II

Funding

Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
Structure and Function of Viral ImmunoevasinsZIAAI001028 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI MARGULIES, DAVID · 2009 to 2025
$7.9M
Biophysical Characterization Of MacromoleculesZIAEB000008 · NIBIB · NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING · PI SCHUCK, PETER · 2009 to 2019
$1.7M
Intramural NIH HHSNIBIB NIH HHS P30 EB009998
6 · The paper itself

Abstract

Natural killer (NK) cells are activated by engagement of the NKG2D receptor with ligands on target cells stressed by infection or tumorigenesis. Several human and rodent cytomegalovirus (CMV) immunoevasins down-regulate surface expression of NKG2D ligands. The mouse CMV MHC class I (MHC-I)-like m152/gp40 glycoprotein down-regulates retinoic acid early inducible-1 (RAE1) NKG2D ligands as well as host MHC-I. Here we describe the crystal structure of an m152/RAE1γ complex and confirm the intermolecular contacts by mutagenesis. m152 interacts in a pincer-like manner with two sites on the α1 and α2 helices of RAE1 reminiscent of the NKG2D interaction with RAE1. This structure of an MHC-I-like immunoevasin/MHC-I-like ligand complex explains the binding specificity of m152 for RAE1 and allows modeling of the interaction of m152 with classical MHC-I and of related viral immunoevasins.

Indexed as

AnimalsDrosophilaEscherichia coliGene Expression Regulation, ViralHEK293 CellsHumansImmune SystemKiller Cells, NaturalLigandsMajor Histocompatibility ComplexMembrane GlycoproteinsMiceMolecular ConformationMuromegalovirusMutationNK Cell Lectin-Like Receptor Subfamily KKLRK1 protein, humanKlrk1 protein, mouseLigandsm152 protein, cytomegalovirusMembrane GlycoproteinsNK Cell Lectin-Like Receptor Subfamily KNuclear Matrix-Associated ProteinsNucleocytoplasmic Transport ProteinsProtein IsoformsRAE1 protein, humanRae1 protein, mouseViral Proteins

Identifiers

PMID23169621
PMCPMC3529088
OpenAlexW1993958616

What Socratic 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 Socratic graph.