Evidence map›Paper›PMID 34273351›Full record

ArticleThe Journal of biological chemistry2021

Structural details of monoclonal antibody m971 recognition of the membrane-proximal domain of CD22.

June Ereño-Orbea, Xianglei Liu, Taylor Sicard, Iga Kucharska, Wei Li, Dorota Borovsky, Hong Cui, Yang Feng, Dimiter S Dimitrov, Jean-Philippe Julien

Open access · goldAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.0field-weighted citation impact, top 21% 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

15 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Review
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  5. Sequence and structural determinants of efficaciousbioRxiv : the preprint server for biology · 2025
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  10. Strategies and rules for tuning TCR-derived therapy.Expert reviews in molecular medicine · 2023
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
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.

June Ereño-OrbeaProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, Ontario, Canada; Ikerbasque, Basque Foundation for Science, Bilbao, Bizkaia, Spain.
Xianglei LiuDivision of Infectious Diseases, Department of Medicine, University of Pittsburgh, Pennsylvania, USA.
Taylor SicardProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, Ontario, Canada; Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada.
Iga KucharskaProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, Ontario, Canada.
Wei LiDivision of Infectious Diseases, Department of Medicine, University of Pittsburgh, Pennsylvania, USA.
Dorota BorovskyDepartment of Immunology, University of Toronto, Toronto, Ontario, Canada.
Hong CuiProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, Ontario, Canada.
Yang FengProtein Interactions Group, Center for Cancer Research Nanobiology Program, Center for Cancer Research, National Institutes of Health, Frederick, Maryland, USA.
Dimiter S DimitrovDivision of Infectious Diseases, Department of Medicine, University of Pittsburgh, Pennsylvania, USA.
Jean-Philippe JulienProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, Ontario, Canada; Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada; Department of Immunology, University of Toronto, Toronto, Ontario, Canada. Electronic address: jean-philippe.julien@sickkids.ca.
University of Pittsburgh · USUniversity of Toronto · CAHospital for Sick Children · CAIkerbasque · ESNational Institutes of Health · US

Funding

CIHR BPF-144483CIHR PJT-148811
6 · The paper itself

Abstract

Cluster of differentiation-22 (CD22) belongs to the sialic acid-binding immunoglobulin (Ig)-like lectin family of receptors that is expressed on the surface of B cells. It has been classified as an inhibitory coreceptor for the B-cell receptor because of its function in establishing a baseline level of B-cell inhibition. The restricted expression of CD22 on B cells and its inhibitory function make it an attractive target for B-cell depletion in cases of B-cell malignancies. Genetically modified T cells with chimeric antigen receptors (CARs) derived from the m971 antibody have shown promise when used as an immunotherapeutic agent against B-cell acute lymphoblastic leukemia. A key aspect of the efficacy of this CAR-T was its ability to target a membrane-proximal epitope on the CD22 extracellular domain; however, the molecular details of m971 recognition of CD22 have thus far remained elusive. Here, we report the crystal structure of the m971 fragment antigen-binding in complex with the two most membrane-proximal Ig-like domains of CD22 (CD22

Indexed as

Sialic Acid Binding Ig-like Lectin 2Antibodies, MonoclonalCrystallography, X-RayEpitopesHumansProtein DomainsAntibodies, MonoclonalCD22 protein, humanEpitopesSialic Acid Binding Ig-like Lectin 2antibodyB cellCAR-T cellCD22crystal structurem971

Identifiers

PMID34273351
PMCPMC8353475
OpenAlexW3182197846

What OpenQuestion holds

Textmetadata
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.