Evidence map›Paper›PMID 32103252›Full record

ReviewGlycobiology2020

Understanding the role of antibody glycosylation through the lens of severe viral and bacterial diseases.

Edward B Irvine, Galit Alter

Open access · hybridAbstract readReview
In one paragraph

Review in Glycobiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed, 1 pooled it
9.7field-weighted citation impact, top 1% 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

87 citing papers in PubMed, 1 synthesis or guideline pooled it, 135 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Acute vascular redox modulation by SGLT2 inhibition in non-diabetic patients.Cardiovascular diabetology. Endocrinology reports · 2026
    Article
  9. Article
  10. Article
  11. Article
  12. Glycan Structures of Human Immunoglobulins and Their Roles.Advances in experimental medicine and biology · 2026
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Article
  20. Article

27 more citing papers are in PubMed but not listed here.

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

2 authors at 2 institutions in 1 country.

Edward B IrvineRagon Institute of MGH, MIT, and Harvard, Cambridge, MA, USA.
Galit AlterRagon Institute of MGH, MIT, and Harvard, Cambridge, MA, USA.
Harvard University · USRagon Institute of MGH, MIT and Harvard · US

Funding

Bacteriology PhD Training ProgramT32AI132120 · NIAID · HARVARD MEDICAL SCHOOL · PI RUDNER, DAVID Z · 2017 to 2021
$1.7M
NIAID NIH HHS T32 AI132120
6 · The paper itself

Abstract

Abundant evidence points to a critical role for antibodies in protection and pathology across infectious diseases. While the antibody variable domain facilitates antibody binding and the blockade of infection, the constant domain (Fc) mediates cross talk with the innate immune system. The biological activity of the Fc region is controlled genetically via class switch recombination, resulting in the selection of distinct antibody isotypes and subclasses. However, a second modification is made to all antibodies, via post-translational changes in antibody glycosylation. Studies from autoimmunity and oncology have established the role of immunoglobulin G (IgG) Fc glycosylation as a key regulator of humoral immune activity. However, a growing body of literature, exploring IgG Fc glycosylation through the lens of infectious diseases, points to the role of inflammation in shaping Fc-glycan profiles, the remarkable immune plasticity in antibody glycosylation across pathogen-exposed populations, the canonical and noncanonical functions of glycans and the existence of antigen-specific control over antibody Fc glycosylation. Ultimately, this work provides critical new insights into the functional roles for antibody glycosylation as well as lays the foundation for leveraging antibody glycosylation to drive prevention or control across diseases.

Indexed as

AnimalsAntibodiesBacterial InfectionsGlycosylationHumansImmunoglobulin Fc FragmentsPolysaccharidesVirus DiseasesAntibodiesImmunoglobulin Fc FragmentsPolysaccharidesantibodyFcglycosylationhumoral immunityinfectious disease

Identifiers

PMID32103252
PMCPMC7109349
OpenAlexW3007860422

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.