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Conformational epitopes of pemphigus antigens (Dsg1 and Dsg3) are calcium dependent and glycosylation independent.
- Source :
-
The Journal of investigative dermatology [J Invest Dermatol] 1995 Aug; Vol. 105 (2), pp. 243-7. - Publication Year :
- 1995
-
Abstract
- The target molecule of pemphigus autoantibodies is a transmembrane desmosomal component, desmoglein 3 (Dsg3) in pemphigus vulgaris (PV) and Dsg1 in pemphigus foliaceus (PF). In this study, we examined the effects of calcium and glycosylation on the anti-genicity of the pemphigus antigens and on the generation of conformational epitopes. We used recombinant baculovirus proteins, PVIg and PFIg, which are considered to reflect accurately the native conformation of the extracellular domain of their respective proteins Dsg3 and Dsg1. These baculoproteins could immunoadsorb heterogeneous autoantibodies from the corresponding sera of PV and PF patients, completely blocking indirect immunofluorescence staining of normal human skin. Chelating calcium from the solution containing the baculoproteins using ethylenediaminetetraacetic acid (EDTA) or ethyleneglycol-bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid (EGTA) abolished immunoadsorption by both PVIg and PFIg; however, immunoadsorption by the baculoproteins was restored after dialysis against 1 mM calcium. Nonglycosylated forms of both baculoproteins produced in the presence of tunicamycin retained their immunoadsorptive ability. Furthermore, immunoadsorption by the baculo-proteins was prevented irreversibly by treatment with low pH, high pH, and boiling, but not with the non-ionic detergent Nonidet P-40. These findings indicate that formation of the conformational epitopes on the pemphigus antigens is dependent on calcium but independent of glycosylation, and provide direct evidence that calcium plays an important role in determining the antigenic properties of the pemphigus antigens.
- Subjects :
- Adsorption
Cadherins chemistry
Cytoskeletal Proteins chemistry
Desmoglein 1
Desmoglein 3
Desmogleins
Desmoplakins
Fluorescent Antibody Technique
Glycosylation
Hot Temperature
Humans
Hydrogen-Ion Concentration
Immunoblotting
Molecular Conformation
Pemphigus blood
Cadherins immunology
Cadherins physiology
Calcium physiology
Cytoskeletal Proteins immunology
Cytoskeletal Proteins physiology
Epitopes
Subjects
Details
- Language :
- English
- ISSN :
- 0022-202X
- Volume :
- 105
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- The Journal of investigative dermatology
- Publication Type :
- Academic Journal
- Accession number :
- 7543549
- Full Text :
- https://doi.org/10.1111/1523-1747.ep12317587