Evidence map›Paper›PMID 30204750›Full record

ArticlePloS one2018

Characterization of neutralizing antibodies reacting with the 213-224 amino-acid segment of human galectin-9.

Claire Lhuillier, Clément Barjon, Valentin Baloche, Toshiro Niki, Aurore Gelin, Rami Mustapha, Laetitia Claër, Sylviane Hoos, Yoichi Chiba, Masaki Ueno and 7 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.4field-weighted citation impact, top 40% 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

11 citing papers in PubMed, 15 citations in OpenAlex.

  1. Galectin-9-An Emerging Glyco-Immune Checkpoint Target for Cancer Therapy.International journal of molecular sciences · 2025
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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

17 authors at 5 institutions in 2 countries.

Claire LhuillierCNRS, UMR 8126, Villejuif, France.
Clément BarjonCNRS, UMR 8126, Villejuif, France.
Valentin BalocheCNRS, UMR 8126, Villejuif, France.
Toshiro NikiDepartment of Immunology, Faculty of Medicine, Kagawa University, Takamatsu, Kagawa, Japan.
Aurore GelinCNRS, UMR 8126, Villejuif, France.
Rami MustaphaCNRS, UMR 8161, IRCV group, Institut de Biologie de Lille, Lille, France.
Laetitia ClaërH-Immune Therapeutics, Paris, France.
Sylviane HoosPlate-forme de Biophysique Moléculaire, Institut Pasteur, Paris, France.
Yoichi ChibaDepartment of Pathology and Host Defense, Faculty of Medicine, Kagawa University, Takamatsu, Kagawa, Japan.
Masaki UenoDepartment of Pathology and Host Defense, Faculty of Medicine, Kagawa University, Takamatsu, Kagawa, Japan.
Mitsuomi HirashimaGalPharma Co., Ltd., Takamatsu, Kagawa, Japan.
Ming WeiCellvax, Romainville, France.
Olivier MoralesCNRS, UMR 8161, IRCV group, Institut de Biologie de Lille, Lille, France.
Bertrand RaynalPlate-forme de Biophysique Moléculaire, Institut Pasteur, Paris, France.
Nadira DelhemCNRS, UMR 8161, IRCV group, Institut de Biologie de Lille, Lille, France.
Olivier DellisINSERM, UMR-S 1174, Univ Paris Sud, Université Paris-Saclay, Orsay, France.
Pierre BussonCNRS, UMR 8126, Villejuif, France.ORCID 0000-0003-1027-3400
Centre National de la Recherche Scientifique · FRKagawa University · JPInstitut Pasteur · FRHiFiBiO Therapeutics (France) · FRInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Extra-cellular galectin-9 (gal-9) is an immuno-modulatory protein with predominant immunosuppressive effects. Inappropriate production of gal-9 has been reported in several human malignancies and viral diseases like nasopharyngeal, pancreatic and renal carcinomas, metastatic melanomas and chronic active viral hepatitis. Therefore therapeutic antibodies neutralizing extra-cellular gal-9 are expected to contribute to immune restoration in these pathological conditions. Two novel monoclonal antibodies targeting gal-9 -Gal-Nab 1 and 2-have been produced and characterized in this study. We report a protective effect of Gal-Nab1 and Gal-Nab2 on the apoptotic cell death induced by gal-9 in primary T cells. In addition, they inhibit late phenotypic changes observed in peripheral T cells that survive gal-9-induced apoptosis. Gal-Nab1 and Gal-Nab2 bind nearly identical, overlapping linear epitopes contained in the 213-224 amino-acid segments of gal-9. Nevertheless, they have some distinct functional characteristics suggesting that their three-dimensional epitopes are distinct. These differences are best demonstrated when gal-9 is applied on Jurkat cells where Gal-Nab1 is less efficient than Gal-Nab2 in the prevention of apoptotic cell death. In addition, Gal-Nab1 stimulates non-lethal phosphatidylserine translocation at the plasma membrane and calcium mobilization triggered by gal-9 in these cells. Both Gal-Nab1 and 2 cross-react with murine gal-9. They bind its natural as well as its recombinant form. This cross-species recognition will be an advantage for their assessment in pre-clinical tumor models.

Indexed as

AnimalsAntibodies, MonoclonalAntibodies, NeutralizingApoptosisBiological TransportCalciumEpitopesGalectinsHumansImmunizationJurkat CellsMicePhosphatidylserinesT-LymphocytesAntibodies, MonoclonalAntibodies, NeutralizingCalciumEpitopesGalectinsLGALS9 protein, humanPhosphatidylserines

Identifiers

PMID30204750
PMCPMC6133441
OpenAlexW2890071829

What OpenQuestion holds

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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.