TY - JOUR
T1 - Monoclonal Antibody to Rubella Virus Capsid Protein Recognizes a β-Cell Antigen
AU - Karounos, D. G.
AU - Wolinsky, J. S.
AU - Thomas, J. W.
PY - 1993
Y1 - 1993
N2 - The high frequency of insulin-dependent diabetes (IDDM) in children with congenital rubella suggests that the infectious agent may trigger the autoimmune process. To explore the immunologie relationship between rubella virus IDDM, we examined a panel of mAb that recognizes rubella virus capsid and envelope glycoproteins for reactivity with islet cell Ag. One mAb, C9, which recognizes a defined domain within the capsid protein of rubella virus, was found to react with extracts from a rat β-cell tumor and normal rat and human islets. Using one and two dimensional immunoblot analysis of rat β-cell tumor extracts, the C9-like epitope was found to reside on a 52 kDa protein that is also the target of autoantibodies from human IDDM and nonobese diabetic mice. To confirm this cross-reactivity, antibodies in diabetic sera were adsorbed to the recombinant rubella virus capsid protein, eluted, and then shown to react with the 52 kDa insulinoma protein. These data show that an immunogenic epitope on the rubella virus capsid protein is mimicked by a similar structure on a β-cell protein. These findings suggest that rubella virus has the potential to sensitize susceptible individuals for an autoimmune response to β-cell Ag and identify one mechanism that may contribute to β destruction in IDDM.
AB - The high frequency of insulin-dependent diabetes (IDDM) in children with congenital rubella suggests that the infectious agent may trigger the autoimmune process. To explore the immunologie relationship between rubella virus IDDM, we examined a panel of mAb that recognizes rubella virus capsid and envelope glycoproteins for reactivity with islet cell Ag. One mAb, C9, which recognizes a defined domain within the capsid protein of rubella virus, was found to react with extracts from a rat β-cell tumor and normal rat and human islets. Using one and two dimensional immunoblot analysis of rat β-cell tumor extracts, the C9-like epitope was found to reside on a 52 kDa protein that is also the target of autoantibodies from human IDDM and nonobese diabetic mice. To confirm this cross-reactivity, antibodies in diabetic sera were adsorbed to the recombinant rubella virus capsid protein, eluted, and then shown to react with the 52 kDa insulinoma protein. These data show that an immunogenic epitope on the rubella virus capsid protein is mimicked by a similar structure on a β-cell protein. These findings suggest that rubella virus has the potential to sensitize susceptible individuals for an autoimmune response to β-cell Ag and identify one mechanism that may contribute to β destruction in IDDM.
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M3 - Article
C2 - 8454875
AN - SCOPUS:0027316131
SN - 0022-1767
VL - 150
SP - 3080
EP - 3085
JO - Journal of Immunology
JF - Journal of Immunology
IS - 7
ER -