CH2 and CH3 domain deleted IgG1 paraproteins inhibit differently Fc receptor mediated binding and cytolysis

G. Sármay, Roy Jefferis, J. Gergely

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Domain deleted paraproteins are suitable tools to study the interaction between IgG domains and Fc receptor (FcR) binding sites. The effect of the Cγ2 or Cγ3 domain deleted paraproteins was compared on antibody dependent cellular cytotoxicity (ADCC) and on FcR mediated rosette formation. The Cγ2 domain deleted paraprotein (TIM) had no significant effect on lymphocyte or monocyte mediated ADCC, while the Cγ3 domain deleted paraprotein (SIZ) inhibited both types of cytotoxicity. FcR dependent rosette formation was also inhibited by SIZ but TIM was ineffective. The data further confirm our previous results suggesting a significant role of Cγ2 domain in the transfer of killing signal in ADCC and that of Cγ3 domain in the high affinity binding to lymphocyte FCR.

Original languageEnglish
Pages (from-to)307-312
Number of pages6
JournalImmunology Letters
Volume12
Issue number5-6
DOIs
Publication statusPublished - 1986

Fingerprint

Paraproteins
Fc Receptors
Immunoglobulin G
Rosette Formation
Antibodies
Lymphocytes
IgG Receptors
Monocytes
Binding Sites
C2 Domains

Keywords

  • antibody dependent cellular cytotoxicity
  • Fc receptor binding sites
  • IgG domains

ASJC Scopus subject areas

  • Immunology
  • Immunology and Allergy

Cite this

CH2 and CH3 domain deleted IgG1 paraproteins inhibit differently Fc receptor mediated binding and cytolysis. / Sármay, G.; Jefferis, Roy; Gergely, J.

In: Immunology Letters, Vol. 12, No. 5-6, 1986, p. 307-312.

Research output: Contribution to journalArticle

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