Advanced

Binding of human and animal immunoglobulins to the IgG Fc receptor induced by human cytomegalovirus

Antonsson, Annika LU and Johansson, Hugo LU (2001) In Journal of General Virology 82(5). p.1137-1145
Abstract
Human cytomegalovirus (HCMV)-infected cells express a virus-encoded receptor that is able to bind the Fc part of IGG: Some basic binding properties of this Fc receptor (FcR) have been examined. The affinity constant (K(a)) for human IgG Fc fragment in its interaction with acetone-fixed, HCMV-infected human embryonic lung fibroblasts was estimated to be around 2 x 10(8) M(-1) and the number of binding sites was estimated to be around 2 x 10(6) per cell. Of the human IgG, IgA, IgM and IgD classes, only IgG reacted with the receptor, and all four of the IgG subclasses were reactive. IgG from rabbit, hamster, cat, swine and horse exhibited binding to the HCMV FcR, in contrast to IgG from mouse, rat, guinea pig, dog, sheep, goat, cow and... (More)
Human cytomegalovirus (HCMV)-infected cells express a virus-encoded receptor that is able to bind the Fc part of IGG: Some basic binding properties of this Fc receptor (FcR) have been examined. The affinity constant (K(a)) for human IgG Fc fragment in its interaction with acetone-fixed, HCMV-infected human embryonic lung fibroblasts was estimated to be around 2 x 10(8) M(-1) and the number of binding sites was estimated to be around 2 x 10(6) per cell. Of the human IgG, IgA, IgM and IgD classes, only IgG reacted with the receptor, and all four of the IgG subclasses were reactive. IgG from rabbit, hamster, cat, swine and horse exhibited binding to the HCMV FcR, in contrast to IgG from mouse, rat, guinea pig, dog, sheep, goat, cow and chicken. Immunoglobulins with and without HCMV IgG FcR-binding properties, like IgG from rabbit and mouse, can be of value in revealing the functional importance of the receptor. When the immunoglobulins were tested against herpes simplex virus type 1-induced FcR, both similarities and differences in immunoreactivity were seen relative to the HCMV FcR, which makes it unlikely that the binding sites for these two herpesvirus FcRs on the IgG molecule are identical. (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
Journal of General Virology
volume
82
issue
5
pages
1137 - 1145
publisher
Society for General Microbiology
external identifiers
  • pmid:11297688
  • scopus:0034996845
ISSN
1465-2099
language
English
LU publication?
yes
id
f9080cca-5791-4030-a6b7-20fe64f19962 (old id 1120886)
date added to LUP
2008-06-23 16:40:42
date last changed
2018-01-07 08:55:04
@article{f9080cca-5791-4030-a6b7-20fe64f19962,
  abstract     = {Human cytomegalovirus (HCMV)-infected cells express a virus-encoded receptor that is able to bind the Fc part of IGG: Some basic binding properties of this Fc receptor (FcR) have been examined. The affinity constant (K(a)) for human IgG Fc fragment in its interaction with acetone-fixed, HCMV-infected human embryonic lung fibroblasts was estimated to be around 2 x 10(8) M(-1) and the number of binding sites was estimated to be around 2 x 10(6) per cell. Of the human IgG, IgA, IgM and IgD classes, only IgG reacted with the receptor, and all four of the IgG subclasses were reactive. IgG from rabbit, hamster, cat, swine and horse exhibited binding to the HCMV FcR, in contrast to IgG from mouse, rat, guinea pig, dog, sheep, goat, cow and chicken. Immunoglobulins with and without HCMV IgG FcR-binding properties, like IgG from rabbit and mouse, can be of value in revealing the functional importance of the receptor. When the immunoglobulins were tested against herpes simplex virus type 1-induced FcR, both similarities and differences in immunoreactivity were seen relative to the HCMV FcR, which makes it unlikely that the binding sites for these two herpesvirus FcRs on the IgG molecule are identical.},
  author       = {Antonsson, Annika and Johansson, Hugo},
  issn         = {1465-2099},
  language     = {eng},
  number       = {5},
  pages        = {1137--1145},
  publisher    = {Society for General Microbiology},
  series       = {Journal of General Virology},
  title        = {Binding of human and animal immunoglobulins to the IgG Fc receptor induced by human cytomegalovirus},
  volume       = {82},
  year         = {2001},
}