The role of carbohydrates in the IgG binding and suppressive activities of shed human Fc receptors

M. Sandor, A. Erdei, U. Blank, C. Néauport-Sautès, W. H. Fridman, J. Gergely

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

IgG Fc receptor (FcγR) shed from human periperal mononuclear cells and purified by IgG affinity chromatography bound to ConA, Pisum sativum, Ulex europeus and peanut lectins. The soluble FcγR was not absorbed by wheat germ, soyabean, lentil, Sophora japonica or Helix pomotia lectins. Out of 14 different sugars, none interfered with the interaction between IgG Fc and membrane FcγR. These results show that shed FcγR had glucosyl, mannosyl, fucosyl and galactosyl groups, but that these components were not part of the IgG-binding site(s). The shed FcR had IgG-binding factor (BF) activity; it suppressed secondary in vitro antibody production. In accordance with the binding studies, IgG-BF activity could be adsorbed by ConA and PNA, but not by lentil lectins. The presence of 10 mM galactose or α-methylmannoside had no influence on biological activity, suggesting that, although present on human shed FcγR, these sugars do not play a major role in its suppressive activity.

Original languageEnglish
Pages (from-to)79-91
Number of pages13
JournalAnnales de l'Institut Pasteur - Immunology
Volume137
Issue number1 D
Publication statusPublished - 1986

Fingerprint

Fc Receptors
Human Activities
Immunoglobulin G
Carbohydrates
Sophora
Ulex
Peanut Agglutinin
Lens Plant
IgG Receptors
Peas
Galactose
Affinity Chromatography
Triticum
Antibody Formation
Binding Sites
Membranes

ASJC Scopus subject areas

  • Medicine(all)

Cite this

The role of carbohydrates in the IgG binding and suppressive activities of shed human Fc receptors. / Sandor, M.; Erdei, A.; Blank, U.; Néauport-Sautès, C.; Fridman, W. H.; Gergely, J.

In: Annales de l'Institut Pasteur - Immunology, Vol. 137, No. 1 D, 1986, p. 79-91.

Research output: Contribution to journalArticle

@article{abd05b81141b48a2a5a0d05431af6a82,
title = "The role of carbohydrates in the IgG binding and suppressive activities of shed human Fc receptors",
abstract = "IgG Fc receptor (FcγR) shed from human periperal mononuclear cells and purified by IgG affinity chromatography bound to ConA, Pisum sativum, Ulex europeus and peanut lectins. The soluble FcγR was not absorbed by wheat germ, soyabean, lentil, Sophora japonica or Helix pomotia lectins. Out of 14 different sugars, none interfered with the interaction between IgG Fc and membrane FcγR. These results show that shed FcγR had glucosyl, mannosyl, fucosyl and galactosyl groups, but that these components were not part of the IgG-binding site(s). The shed FcR had IgG-binding factor (BF) activity; it suppressed secondary in vitro antibody production. In accordance with the binding studies, IgG-BF activity could be adsorbed by ConA and PNA, but not by lentil lectins. The presence of 10 mM galactose or α-methylmannoside had no influence on biological activity, suggesting that, although present on human shed FcγR, these sugars do not play a major role in its suppressive activity.",
author = "M. Sandor and A. Erdei and U. Blank and C. N{\'e}auport-Saut{\`e}s and Fridman, {W. H.} and J. Gergely",
year = "1986",
language = "English",
volume = "137",
pages = "79--91",
journal = "Annales de l'Institut Pasteur - Immunology",
issn = "0769-2625",
publisher = "Elsevier BV",
number = "1 D",

}

TY - JOUR

T1 - The role of carbohydrates in the IgG binding and suppressive activities of shed human Fc receptors

AU - Sandor, M.

AU - Erdei, A.

AU - Blank, U.

AU - Néauport-Sautès, C.

AU - Fridman, W. H.

AU - Gergely, J.

PY - 1986

Y1 - 1986

N2 - IgG Fc receptor (FcγR) shed from human periperal mononuclear cells and purified by IgG affinity chromatography bound to ConA, Pisum sativum, Ulex europeus and peanut lectins. The soluble FcγR was not absorbed by wheat germ, soyabean, lentil, Sophora japonica or Helix pomotia lectins. Out of 14 different sugars, none interfered with the interaction between IgG Fc and membrane FcγR. These results show that shed FcγR had glucosyl, mannosyl, fucosyl and galactosyl groups, but that these components were not part of the IgG-binding site(s). The shed FcR had IgG-binding factor (BF) activity; it suppressed secondary in vitro antibody production. In accordance with the binding studies, IgG-BF activity could be adsorbed by ConA and PNA, but not by lentil lectins. The presence of 10 mM galactose or α-methylmannoside had no influence on biological activity, suggesting that, although present on human shed FcγR, these sugars do not play a major role in its suppressive activity.

AB - IgG Fc receptor (FcγR) shed from human periperal mononuclear cells and purified by IgG affinity chromatography bound to ConA, Pisum sativum, Ulex europeus and peanut lectins. The soluble FcγR was not absorbed by wheat germ, soyabean, lentil, Sophora japonica or Helix pomotia lectins. Out of 14 different sugars, none interfered with the interaction between IgG Fc and membrane FcγR. These results show that shed FcγR had glucosyl, mannosyl, fucosyl and galactosyl groups, but that these components were not part of the IgG-binding site(s). The shed FcR had IgG-binding factor (BF) activity; it suppressed secondary in vitro antibody production. In accordance with the binding studies, IgG-BF activity could be adsorbed by ConA and PNA, but not by lentil lectins. The presence of 10 mM galactose or α-methylmannoside had no influence on biological activity, suggesting that, although present on human shed FcγR, these sugars do not play a major role in its suppressive activity.

UR - http://www.scopus.com/inward/record.url?scp=0022588025&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0022588025&partnerID=8YFLogxK

M3 - Article

C2 - 2944472

AN - SCOPUS:0022588025

VL - 137

SP - 79

EP - 91

JO - Annales de l'Institut Pasteur - Immunology

JF - Annales de l'Institut Pasteur - Immunology

SN - 0769-2625

IS - 1 D

ER -