Evidence map›Paper›PMID 22802125›Full record

ArticleCellular and molecular life sciences : CMLS2012

Multimeric structures of HLA-G isoforms function through differential binding to LILRB receptors.

Kiave-Yune HoWangYin, Maria Loustau, Juan Wu, Estibaliz Alegre, Marina Daouya, Julien Caumartin, Sylvie Sousa, Anatolij Horuzsko, Edgardo D Carosella, Joel LeMaoult

Abstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed, 1 pooled it
2.4field-weighted citation impact, top 11% 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

51 citing papers in PubMed, 1 synthesis or guideline pooled it, 82 citations in OpenAlex.

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  15. An HLA-G/SPAG9/STAT3 axis promotes brain metastases.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

10 authors at 5 institutions in 3 countries.

Kiave-Yune HoWangYinCEA, Institute of Emerging Diseases and Innovative Therapies (iMETI), Research Division in Hematology and Immunology (SRHI), Saint-Louis Hospital, 1 Avenue Claude Vellefaux, 75475, Paris, France.
Maria Loustau
Juan Wu
Estibaliz Alegre
Marina Daouya
Julien Caumartin
Sylvie Sousa
Anatolij Horuzsko
Edgardo D Carosella
Joel LeMaoult
Commissariat à l'Énergie Atomique et aux Énergies Alternatives · FRAugusta University Health · USDélégation Paris 7 · FRClinica Universidad de Navarra · ESHôpital Saint-Louis · FR

Funding

Potential of HLA-G for TransplantationR56AI055923 · NIAID · AUGUSTA UNIVERSITY · PI HORUZSKO, ANATOLIJ · 2009 to 2009
$331k
NIAID NIH HHS R56 AI055923
6 · The paper itself

Abstract

The non-classical Human leukocyte antigen G (HLA-G) differs from classical HLA class I molecules by its low genetic diversity, a tissue-restricted expression, the existence of seven isoforms, and immuno-inhibitory functions. Most of the known functions of HLA-G concern the membrane-bound HLA-G1 and soluble HLA-G5 isoforms, which present the typical structure of classical HLA class I molecule: a heavy chain of three globular domains α1-α2-α3 non-covalently bound to β-2-microglobulin (B2M) and a peptide. Very little is known of the structural features and functions of other HLA-G isoforms or structural conformations other than B2M-associated HLA-G1 and HLA-G5. In the present work, we studied the capability of all isoforms to form homomultimers, and investigated whether they could bind to, and function through, the known HLA-G receptors LILRB1 and LILRB2. We report that all HLA-G isoforms may form homodimers, demonstrating for the first time the existence of HLA-G4 dimers. We also report that the HLA-G α1-α3 structure, which constitutes the extracellular part of HLA-G2 and HLA-G6, binds the LILRB2 receptor but not LILRB1. This is the first report of a receptor for a truncated HLA-G isoform. Following up on this finding, we show that the α1-α3-Fc structure coated on agarose beads is tolerogenic and capable of prolonging the survival of skin allografts in B6-mice and in a LILRB2-transgenic mouse model. This study is the first proof of concept that truncated HLA-G isoforms could be used as therapeutic agents.

Indexed as

AnimalsAntigens, CDbeta 2-MicroglobulinBinding, CompetitiveBlotting, WesternCell Line, TumorFlow CytometryGraft SurvivalHEK293 CellsHeLa CellsHistocompatibility Antigens Class IHLA-G AntigensHumansKaplan-Meier EstimateLeukocyte Immunoglobulin-like Receptor B1Membrane GlycoproteinsAntigens, CDbeta 2-MicroglobulinHistocompatibility Antigens Class IHLA-G AntigensLeukocyte Immunoglobulin-like Receptor B1LILRB1 protein, humanLILRB2 protein, humanMembrane GlycoproteinsProtein IsoformsReceptors, Immunologic

Identifiers

PMID22802125
PMCPMC3884069
OpenAlexW2167577087

What OpenQuestion holds

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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.