Advanced

A Monosaccharide Residue Is Sufficient to Maintain Mouse and Human IgG Subclass Activity and Directs IgG Effector Functions to Cellular Fc Receptors.

Kao, Daniela; Danzer, Heike; Collin, Mattias LU ; Groß, Andrea; Eichler, Jutta; Stambuk, Jerko; Lauc, Gordan; Lux, Anja and Nimmerjahn, Falk (2015) In Cell Reports 13(11). p.2376-2385
Abstract
Immunoglobulin G (IgG) glycosylation modulates antibody activity and represents a major source of heterogeneity within antibody preparations. Depending on their glycosylation pattern, individual IgG glycovariants present in recombinant antibody preparations may trigger effects ranging from enhanced pro-inflammatory activity to increased anti-inflammatory activity. In contrast, reduction of IgG glycosylation beyond the central mannose core is generally believed to result in impaired IgG activity. However, this study reveals that a mono- or disaccharide structure consisting of one N-acetylglucosamine with or without a branching fucose residue is sufficient to retain the activity of the most active human and mouse IgG subclasses in vivo and... (More)
Immunoglobulin G (IgG) glycosylation modulates antibody activity and represents a major source of heterogeneity within antibody preparations. Depending on their glycosylation pattern, individual IgG glycovariants present in recombinant antibody preparations may trigger effects ranging from enhanced pro-inflammatory activity to increased anti-inflammatory activity. In contrast, reduction of IgG glycosylation beyond the central mannose core is generally believed to result in impaired IgG activity. However, this study reveals that a mono- or disaccharide structure consisting of one N-acetylglucosamine with or without a branching fucose residue is sufficient to retain the activity of the most active human and mouse IgG subclasses in vivo and further directs antibody activity to cellular Fcγ receptors. Notably, the activity of minimally glycosylated antibodies is not predicted by in vitro assays based on a monomeric antibody-Fcγ-receptor interaction analysis, whereas in vitro assay systems using immune complexes are more suitable to predict IgG activity in vivo. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Cell Reports
volume
13
issue
11
pages
2376 - 2385
publisher
Cell Press
external identifiers
  • pmid:26670049
  • wos:000367101400008
  • scopus:84951291802
ISSN
2211-1247
DOI
10.1016/j.celrep.2015.11.027
language
English
LU publication?
yes
id
56dc7895-7370-4520-a69d-87dcaab05c05 (old id 8504725)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/26670049?dopt=Abstract
date added to LUP
2016-01-05 19:56:33
date last changed
2017-10-22 04:04:34
@article{56dc7895-7370-4520-a69d-87dcaab05c05,
  abstract     = {Immunoglobulin G (IgG) glycosylation modulates antibody activity and represents a major source of heterogeneity within antibody preparations. Depending on their glycosylation pattern, individual IgG glycovariants present in recombinant antibody preparations may trigger effects ranging from enhanced pro-inflammatory activity to increased anti-inflammatory activity. In contrast, reduction of IgG glycosylation beyond the central mannose core is generally believed to result in impaired IgG activity. However, this study reveals that a mono- or disaccharide structure consisting of one N-acetylglucosamine with or without a branching fucose residue is sufficient to retain the activity of the most active human and mouse IgG subclasses in vivo and further directs antibody activity to cellular Fcγ receptors. Notably, the activity of minimally glycosylated antibodies is not predicted by in vitro assays based on a monomeric antibody-Fcγ-receptor interaction analysis, whereas in vitro assay systems using immune complexes are more suitable to predict IgG activity in vivo.},
  author       = {Kao, Daniela and Danzer, Heike and Collin, Mattias and Groß, Andrea and Eichler, Jutta and Stambuk, Jerko and Lauc, Gordan and Lux, Anja and Nimmerjahn, Falk},
  issn         = {2211-1247},
  language     = {eng},
  number       = {11},
  pages        = {2376--2385},
  publisher    = {Cell Press},
  series       = {Cell Reports},
  title        = {A Monosaccharide Residue Is Sufficient to Maintain Mouse and Human IgG Subclass Activity and Directs IgG Effector Functions to Cellular Fc Receptors.},
  url          = {http://dx.doi.org/10.1016/j.celrep.2015.11.027},
  volume       = {13},
  year         = {2015},
}