Evidence map›Paper›PMID 31172182›Full record

ReviewGlycobiology2020

Structural insights into the mechanisms and specificities of IgG-active endoglycosidases.

Jonathan J Du, Erik H Klontz, Marcelo E Guerin, Beatriz Trastoy, Eric J Sundberg

Abstract 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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

  1. Glycan Structures of Human Immunoglobulins and Their Roles.Advances in experimental medicine and biology · 2026
    Review
  2. Article
  3. Immunomodulating Enzymes fromMicroorganisms · 2024
    Review
  4. Article
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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

5 authors.

Jonathan J DuInstitute of Human Virology 725 W Lombard Street, Baltimore, MD 21201, USA.
Erik H KlontzInstitute of Human Virology 725 W Lombard Street, Baltimore, MD 21201, USA.
Marcelo E GuerinStructural Biology Unit, CIC bioGUNE, Bizkaia Technology Park, 48160 Derio, Spain.
Beatriz TrastoyProgram in Molecular Microbiology & Immunology, University of Maryland School of Medicine, 685 West Baltimore Street, HSF-I Suite 380, Baltimore, MD 21201, USA.
Eric J SundbergInstitute of Human Virology 725 W Lombard Street, Baltimore, MD 21201, USA.

Funding

Signaling Pathways in Innate ImmunityT32AI095190 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI Stefanie N. Vogel · 2012 to 2026
$4.7M
Rationalizing glycoengineering strategies for immunotherapeutic antibodiesR01AI149297 · NIAID · EMORY UNIVERSITY · PI JEFFREY Victor RAVETCH, ERIC JOHN SUNDBERG · 2020 to 2026
$3.7M
NIAID NIH HHS R01 AI149297NIAID NIH HHS T32 AI095190
6 · The paper itself

Abstract

The conserved N-glycan on Asn297 of immunoglobulin G (IgG) has significant impacts on antibody effector functions, and is a frequent target for antibody engineering. Chemoenzymatic synthesis has emerged as a strategy for producing antibodies with homogenous glycosylation and improved effector functions. Central to this strategy is the use of enzymes with activity on the Asn297 glycan. EndoS and EndoS2, produced by Streptococcus pyogenes, are endoglycosidases with remarkable specificity for Asn297 glycosylation, making them ideal tools for chemoenzymatic synthesis. Although both enzymes are specific for IgG, EndoS2 recognizes a wider range of glycans than EndoS. Recent progress has been made in understanding the structural basis for their activities on antibodies. In this review, we examine the molecular mechanism of glycosidic bond cleavage by these enzymes and how specific point mutations convert them into glycosynthases. We also discuss the structural basis for differences in the glycan repertoire that IgG-active endoglycosidases recognize, which focuses on the structure of the loops within the glycoside hydrolase (GH) domain. Finally, we discuss the important contributions of carbohydrate binding modules (CBMs) to endoglycosidase activity, and how CBMs work in concert with GH domains to produce optimal activity on IgG.

Indexed as

AnimalsGlycoside HydrolasesGlycosylationHumansImmunoglobulin GModels, MolecularMolecular StructurePolysaccharidesStreptococcus pyogenesGlycoside HydrolasesImmunoglobulin GPolysaccharidesantibodyendoglycosidaseEndoSglycosynthaseIgGstructure

Identifiers

PMID31172182
PMCPMC7476101

What OpenQuestion holds

Textmetadata
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.