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The herpes simplex virus type 1 Fc receptor discriminates between IgG1 allotypes
A Atherton1, K L Armour, S Bell
1Department of Pathology, University of Cambridge, GB.
European Journal of Immunology
|September 29, 2000
Summary
The Herpes simplex virus type 1 (HSV-1) Fc receptor (FcR) distinguishes between different allotypes of human immunoglobulin G1 (IgG1). This finding reveals functional differences in IgG1 allotypes, impacting their population distribution.
Area of Science:
- Immunology
- Virology
- Molecular Biology
Background:
- Herpes simplex virus type 1 (HSV-1) produces a glycoprotein complex (gE-gl) functioning as an Fc receptor (FcR).
- This FcR binds nonimmune human IgG, with reported binding preferences for IgG4 > IgG1 > or = IgG2, and typically not IgG3.
- Human IgG1 exhibits allelic variations, known as allotypes, due to genetic differences in the heavy chain constant region.
Purpose of the Study:
- To investigate whether the HSV-1 FcR discriminates between different human IgG1 allotypes.
- To explore potential functional implications of IgG1 allotypes and their population distribution.
Main Methods:
- Utilized recombinant monoclonal IgG molecules with defined isotypes and mutations.
- Tested the binding capabilities of the HSV-1 FcR against these engineered IgG molecules.
Main Results:
- The HSV-1 FcR unexpectedly demonstrated discrimination between different IgG1 allotypes.
- This suggests functional distinctions exist among IgG1 allotypes.
Conclusions:
- The study provides evidence for functional differences between IgG1 allotypes, potentially explaining their varying prevalence in human populations.
- Findings imply that the binding sites for the HSV-1 FcR on IgG molecules may be located away from the previously proposed CH2-CH3 domain interface.