PMID- 25259950
OWN - NLM
STAT- MEDLINE
DCOM- 20150610
LR  - 20211021
IS  - 1932-6203 (Electronic)
IS  - 1932-6203 (Linking)
VI  - 9
IP  - 9
DP  - 2014
TI  - Different IVIG glycoforms affect in vitro inhibition of anti-ganglioside 
      antibody-mediated complement deposition.
PG  - e107772
LID - 10.1371/journal.pone.0107772 [doi]
LID - e107772
AB  - Intravenous immunoglobulin (IVIG) is the first line treatment for Guillain-Barre 
      syndrome and multifocal motor neuropathy, which are caused by anti-ganglioside 
      antibody-mediated complement-dependent cytotoxicity. IVIG has many potential 
      mechanisms of action, and sialylation of the IgG Fc portion reportedly has an 
      anti-inflammatory effect in antibody-dependent cell-mediated cytotoxicity models. 
      We investigated the effects of different IVIG glycoforms on the inhibition of 
      antibody-mediated complement-dependent cytotoxicity. Deglycosylated, 
      degalactosylated, galactosylated and sialylated IgG were prepared from IVIG 
      following treatment with glycosidases and glycosyltransferases. Sera from 
      patients with Guillain-Barre syndrome, Miller Fisher syndrome and multifocal 
      motor neuropathy associated with anti-ganglioside antibodies were used. 
      Inhibition of complement deposition subsequent to IgG or IgM autoantibody binding 
      to ganglioside, GM1 or GQ1b was assessed on microtiter plates. Sialylated and 
      galactosylated IVIGs more effectively inhibited C3 deposition than original IVIG 
      or enzyme-treated IVIGs (agalactosylated and deglycosylated IVIGs). Therefore, 
      sialylated and galactosylated IVIGs may be more effective than conventional IVIG 
      in the treatment of complement-dependent autoimmune diseases.
FAU - Sudo, Makoto
AU  - Sudo M
AD  - Department of Medicine, Yong Loo Lin School of Medicine, National University of 
      Singapore, Singapore, Singapore.
FAU - Yamaguchi, Yoshiki
AU  - Yamaguchi Y
AD  - Structural Glycobiology Team, RIKEN, Wako, Saitama, Japan.
FAU - Spath, Peter J
AU  - Spath PJ
AD  - Institute of Pharmacology, University of Bern, Bern, Switzerland.
FAU - Matsumoto-Morita, Kana
AU  - Matsumoto-Morita K
AD  - Structural Glycobiology Team, RIKEN, Wako, Saitama, Japan.
FAU - Ong, Benjamin K
AU  - Ong BK
AD  - Department of Medicine, Yong Loo Lin School of Medicine, National University of 
      Singapore, Singapore, Singapore.
FAU - Shahrizaila, Nortina
AU  - Shahrizaila N
AD  - Department of Medicine, Faculty of Medicine, University of Malaya, Kuala Lumpur, 
      Malaysia.
FAU - Yuki, Nobuhiro
AU  - Yuki N
AD  - Department of Medicine, Yong Loo Lin School of Medicine, National University of 
      Singapore, Singapore, Singapore; Department of Physiology, Yong Loo Lin School of 
      Medicine, National University of Singapore, Singapore, Singapore.
LA  - eng
GR  - Medical Research Council/United Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20140926
PL  - United States
TA  - PLoS One
JT  - PloS one
JID - 101285081
RN  - 0 (Autoantibodies)
RN  - 0 (Gangliosides)
RN  - 0 (Immunoglobulin G)
RN  - 0 (Immunoglobulins, Intravenous)
RN  - 0 (Polysaccharides)
RN  - 9007-36-7 (Complement System Proteins)
SB  - IM
MH  - Autoantibodies/*immunology
MH  - Complement System Proteins/*immunology/*metabolism
MH  - Gangliosides/antagonists & inhibitors/*immunology
MH  - Glycosylation
MH  - Humans
MH  - Immunoglobulin G/immunology/metabolism/pharmacology
MH  - Immunoglobulins, Intravenous/*immunology/metabolism/pharmacology
MH  - In Vitro Techniques
MH  - Polysaccharides/metabolism
PMC - PMC4178036
COIS- Competing Interests: The authors have declared that no competing interests exist.
EDAT- 2014/09/27 06:00
MHDA- 2015/06/11 06:00
PMCR- 2014/09/26
CRDT- 2014/09/27 06:00
PHST- 2014/04/09 00:00 [received]
PHST- 2014/08/11 00:00 [accepted]
PHST- 2014/09/27 06:00 [entrez]
PHST- 2014/09/27 06:00 [pubmed]
PHST- 2015/06/11 06:00 [medline]
PHST- 2014/09/26 00:00 [pmc-release]
AID - PONE-D-14-15446 [pii]
AID - 10.1371/journal.pone.0107772 [doi]
PST - epublish
SO  - PLoS One. 2014 Sep 26;9(9):e107772. doi: 10.1371/journal.pone.0107772. 
      eCollection 2014.