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|Title:||Common antigenicity for two glycosidases|
|Citation:||FEBS Letters, 2006; 580(1):87-92|
|Publisher:||Elsevier Science BV|
|Revecca Kakavanos, Pierre Lehn, Isabelle Callebaut, Peter J. Meikle, Emma J. Parkinson-Lawrence, John J. Hopwood and Doug A. Brooks|
|Abstract:||Enzyme replacement therapy (ERT) has proven to be an effective therapy for some lysosomal storage disorder (LSD) patients. A potential complication during ERT is the generation of an immune response against the replacement protein. We have investigated the antigenicity of two distantly related glycosidases, alpha-glucosidase (Pompe disease or glycogen storage disease type II, GSD II), and alpha-L-iduronidase (Hurler syndrome, mucopolysaccharidosis type I, MPS I). The linear sequence epitope reactivity of affinity purified polyclonal antibodies to recombinant human alpha-glucosidase and alpha-L-iduronidase was defined, to both glycosidases. The polyclonal antibodies exhibited some cross-reactive epitopes on the two proteins. Moreover, a monoclonal antibody to the active site of alpha-glucosidase showed cross-reactivity with a catalytic structural element of alpha-L-iduronidase. In a previous study, in MPS I patients who developed an immune response to ERT, this same site on alpha-L-iduronidase was highly antigenic and the last to tolerise following repeated enzyme infusions. We conclude that glycosidases can exhibit cross-reactive epitopes, and infer that this may relate to common structural elements associated with their active sites.|
Glycogen Storage Disease Type II
Lysosomal Storage Diseases
Enzyme-Linked Immunosorbent Assay
|Description:||Copyright © 2005 Federation of European Biochemical Societies Published by Elsevier B.V.|
|Appears in Collections:||Aurora harvest 6|
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