Evidence map›Paper›PMID 32273875›Full record

ArticleFrontiers in immunology2020

Removal of Mannose-Ending Glycan at Asn

Sandrine Delignat, Julie Rayes, Suryasarathi Dasgupta, Bagirath Gangadharan, Cécile V Denis, Olivier D Christophe, Jagadeesh Bayry, Srinivas V Kaveri, Sébastien Lacroix-Desmazes

Open access · goldAbstract read
In one paragraph

Article in Frontiers in immunology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.4field-weighted citation impact, top 38% 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

9 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
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  4. Exploration of biomarkers for inhibitor development in persons with hemophilia A.Research and practice in thrombosis and haemostasis · 2025
    Article
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  6. 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

9 authors at 5 institutions in 1 country.

Sandrine DelignatInstitut National de la Santé et de la Recherche Médicale, Centre de Recherche des Cordeliers, Sorbonne Université, Université de Paris, Paris, France.
Julie RayesInstitut National de la Santé et de la Recherche Médicale, Centre de Recherche des Cordeliers, Sorbonne Université, Université de Paris, Paris, France.
Suryasarathi DasguptaInstitut National de la Santé et de la Recherche Médicale, Centre de Recherche des Cordeliers, Sorbonne Université, Université de Paris, Paris, France.
Bagirath GangadharanInstitut National de la Santé et de la Recherche Médicale, Centre de Recherche des Cordeliers, Sorbonne Université, Université de Paris, Paris, France.
Cécile V DenisHITh, UMR_S1176, INSERM, Université Paris-Saclay, Le Kremlin-Bicêtre, France.
Olivier D ChristopheHITh, UMR_S1176, INSERM, Université Paris-Saclay, Le Kremlin-Bicêtre, France.
Jagadeesh BayryInstitut National de la Santé et de la Recherche Médicale, Centre de Recherche des Cordeliers, Sorbonne Université, Université de Paris, Paris, France.
Srinivas V KaveriInstitut National de la Santé et de la Recherche Médicale, Centre de Recherche des Cordeliers, Sorbonne Université, Université de Paris, Paris, France.
Sébastien Lacroix-DesmazesInstitut National de la Santé et de la Recherche Médicale, Centre de Recherche des Cordeliers, Sorbonne Université, Université de Paris, Paris, France.
Inserm · FRSorbonne Université · FRUniversité Paris Cité · FRUniversité Paris-Saclay · FRCentre de Recherche des Cordeliers · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The development of an immune response against therapeutic factor VIII is the major complication in hemophilia A patients. Oligomannose carbohydrates at N239 and/or N2118 on factor VIII allow its binding to the macrophage mannose receptor expressed on human dendritic cells, thereby leading to factor VIII endocytosis and presentation to CD4+ T lymphocytes. Here, we investigated whether altering the interaction of factor VIII with mannose-sensitive receptors on antigen-presenting cells may be a strategy to reduce factor VIII immunogenicity. Gene transfer experiments in factor VIII-deficient mice indicated that N239Q and/or N2118Q factor VIII mutants have similar specific activities as compared to non-mutated factor VIII; N239Q/N2118Q mutant corrected blood loss upon tail clip. Production of the corresponding recombinant FVIII mutants or light chains indicated that removal of the N-linked glycosylation site at N2118 is sufficient to abrogate

Indexed as

AnimalsAntigen PresentationDendritic CellsFactor VIIIHumansLectins, C-TypeLymphocyte ActivationMannoseMannose-Binding LectinsMannose ReceptorMiceMice, Inbred C57BLMice, KnockoutMonocytesMutationReceptors, Cell SurfaceFactor VIIILectins, C-TypeMannoseMannose-Binding LectinsMannose ReceptorReceptors, Cell Surfacefactor VIIIFVIII inhibitorshemophilia Aimmunogenicity of therapeutic proteinsN-glycosylations

Identifiers

PMID32273875
PMCPMC7117063
OpenAlexW3013930695

What OpenQuestion holds

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LicenceCC BY
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.