Major retinal cell components recognized by onchocerciasis sera are associated with the cell surface and nucleoli.
OBJECTIVE
Cellular localization of the components recognized by onchocerciasis autoantibodies has not been investigated in any detail in cultured retinal cells. This study sought to examine, in cultured retinal cells, the subcellular localization of major components that cross-react with onchocerciasis sera.


METHODS
Immunofluorescence confocal laser scanning microscopy and Western blot analysis were carried out on adult pig retinal cells.


RESULTS
The onchocerciasis sera contain antibodies cross-reacting strongly with components of the surface and nucleoli in both the cultured retinal pigment epithelial and neural retinal cells. These epitopes are not recognized by the control sera obtained from noninfected individuals residing in an onchocerciasis hyperendemic area, and from those with or without ocular disease who have never been in any of the onchocerciasis hyperendemic countries. Double-labeling immunofluorescence microscopy does not detect any colocalization of a putative onchocerciasis autoantigen, calreticulin, and those cellular components recognized by onchocerciasis sera in either cell type. Furthermore, none of the onchocerciasis sera tested recognized recombinant calreticulin by Western blot analysis.


CONCLUSIONS
Major epitopes for onchocerciasis anti-retinal autoantibodies are associated with the surface and nucleolus components of retinal cells. Interaction of the onchocerciasis antibodies with the retinal cell surface molecules may play an important role in the development of ocular diseases initiated by the damage of retinal cells. Furthermore, the finding that the cellular components recognized by onchocerciasis sera do not colocalize with calreticulin, taken together with the observation of lack of recognition of recombinant calreticulin by these sera on Western blots, suggests that calreticulin is not a major onchocerciasis autoantigen.
Zhou
Y
Y
Department of Anatomy and Cell Biology, Faculty of Medicine, University of Toronto, Ontario, Canada.
Dziak
E
E
Unnasch
T R
TR
Opas
M
M
D000818:Animals; D000909:Antibodies, Helminth / Q000276:immunology*; D001323:Autoantibodies / Q000276:immunology; D001324:Autoantigens / Q000276:immunology; D015153:Blotting, Western; D002135:Calcium-Binding Proteins / Q000276:immunology; D037282:Calreticulin; D002466:Cell Nucleolus / Q000276:immunology*; D002478:Cells, Cultured; D003429:Cross Reactions / Q000276:immunology; D000939:Epitopes / Q000276:immunology; D005455:Fluorescent Antibody Technique; D006801:Humans; D008565:Membrane Proteins / Q000276:immunology*; D017181:Onchocerca volvulus / Q000276:immunology*; D015827:Onchocerciasis, Ocular / Q000276:immunology*; D010857:Pigment Epithelium of Eye / Q000276:immunology; D012160:Retina / Q000166:cytology / Q000276:immunology*; D012261:Ribonucleoproteins / Q000276:immunology; D013552:Swine
D000909:Antibodies, Helminth; D001323:Autoantibodies; D001324:Autoantigens; D002135:Calcium-Binding Proteins; D037282:Calreticulin; D000939:Epitopes; D008565:Membrane Proteins; D012261:Ribonucleoproteins