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Human immunoglobulin class and subclass specificity of Fc receptors induced by herpes simplex virus type 1

Johansson, Hugo LU ; Hallberg, Torgny LU ; Oxelius, Vivi-Anne LU ; Grubb, Anders LU and Blomberg, Jonas (1984) In Journal of Virology 50(3). p.796-804
Abstract
Herpes simplex virus is known to induce an immunoglobulin-binding cell surface receptor in infected cells that utilizes a nonimmune mechanism. In the present paper, we report the immunoglobulin class and subclass specificity of this receptor. Of the human immunoglobulins G(IgG), IgA, IgM, and IgD, as well as the structurally related beta2 microglobulin, only IgG and its Fc portion exhibited an increased binding to herpes simplex virus-infected cells versus uninfected control cells. The IgG subclass specificity of the Fc receptor was studied in 37 radioiodinated IgG myeloma proteins representing all four subclasses. We found that IgG3 myeloma proteins did not bind to herpes simplex virus-infected cells to a greater extent than to uninfected... (More)
Herpes simplex virus is known to induce an immunoglobulin-binding cell surface receptor in infected cells that utilizes a nonimmune mechanism. In the present paper, we report the immunoglobulin class and subclass specificity of this receptor. Of the human immunoglobulins G(IgG), IgA, IgM, and IgD, as well as the structurally related beta2 microglobulin, only IgG and its Fc portion exhibited an increased binding to herpes simplex virus-infected cells versus uninfected control cells. The IgG subclass specificity of the Fc receptor was studied in 37 radioiodinated IgG myeloma proteins representing all four subclasses. We found that IgG3 myeloma proteins did not bind to herpes simplex virus-infected cells to a greater extent than to uninfected cells. On the contrary, proteins belonging to the other subclasses exhibited an increased binding to herpes simplex virus-infected cells of the following relative magnitude: IgG4 greater than IgG1 greater than or equal to IgG2. This increment of binding could be abolished by addition of a large excess of human IgG Fc fragment. Evidence for the existence of a variable herpes simplex virus-specific binding ability between myeloma proteins belonging to the same IgG subclass was also obtained. Furthermore, we tested two other herpes simplex virus type 1 strains with a limited number of myeloma proteins with very similar results as with the herpes simplex virus type 1 F strain. Several sources of experimental artefacts were controlled, including the state of aggregation of the test proteins, the functional integrity of the Fc portion before and after radioiodination, and the subclass assignments. The implications for the biological role of the Fc receptor of herpes simplex virus are discussed. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Virology
volume
50
issue
3
pages
796 - 804
publisher
American Society for Microbiology
external identifiers
  • pmid:6328009
  • scopus:0021265613
ISSN
1098-5514
language
English
LU publication?
yes
id
7c975ac9-5260-4ce0-b2e2-e6f502f2d622 (old id 1103193)
alternative location
http://www.pubmedcentral.nih.gov/picrender.fcgi?artid=255739&blobtype=pdf
date added to LUP
2008-08-12 14:11:21
date last changed
2017-08-06 04:22:50
@article{7c975ac9-5260-4ce0-b2e2-e6f502f2d622,
  abstract     = {Herpes simplex virus is known to induce an immunoglobulin-binding cell surface receptor in infected cells that utilizes a nonimmune mechanism. In the present paper, we report the immunoglobulin class and subclass specificity of this receptor. Of the human immunoglobulins G(IgG), IgA, IgM, and IgD, as well as the structurally related beta2 microglobulin, only IgG and its Fc portion exhibited an increased binding to herpes simplex virus-infected cells versus uninfected control cells. The IgG subclass specificity of the Fc receptor was studied in 37 radioiodinated IgG myeloma proteins representing all four subclasses. We found that IgG3 myeloma proteins did not bind to herpes simplex virus-infected cells to a greater extent than to uninfected cells. On the contrary, proteins belonging to the other subclasses exhibited an increased binding to herpes simplex virus-infected cells of the following relative magnitude: IgG4 greater than IgG1 greater than or equal to IgG2. This increment of binding could be abolished by addition of a large excess of human IgG Fc fragment. Evidence for the existence of a variable herpes simplex virus-specific binding ability between myeloma proteins belonging to the same IgG subclass was also obtained. Furthermore, we tested two other herpes simplex virus type 1 strains with a limited number of myeloma proteins with very similar results as with the herpes simplex virus type 1 F strain. Several sources of experimental artefacts were controlled, including the state of aggregation of the test proteins, the functional integrity of the Fc portion before and after radioiodination, and the subclass assignments. The implications for the biological role of the Fc receptor of herpes simplex virus are discussed.},
  author       = {Johansson, Hugo and Hallberg, Torgny and Oxelius, Vivi-Anne and Grubb, Anders and Blomberg, Jonas},
  issn         = {1098-5514},
  language     = {eng},
  number       = {3},
  pages        = {796--804},
  publisher    = {American Society for Microbiology},
  series       = {Journal of Virology},
  title        = {Human immunoglobulin class and subclass specificity of Fc receptors induced by herpes simplex virus type 1},
  volume       = {50},
  year         = {1984},
}