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Type: Journal article
Title: Common antigenicity for two glycosidases
Author: Kakavanos, R.
Lehn, P.
Callebaut, I.
Meikle, P.
Parkinson-Lawrence, E.
Hopwood, J.
Brooks, D.
Citation: FEBS Letters, 2006; 580(1):87-92
Publisher: Elsevier Science BV
Issue Date: 2006
ISSN: 0014-5793
Statement of
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.
Keywords: Animals
Glycogen Storage Disease Type II
Mucopolysaccharidosis I
Lysosomal Storage Diseases
Enzyme-Linked Immunosorbent Assay
Epitope Mapping
Description: Copyright © 2005 Federation of European Biochemical Societies Published by Elsevier B.V.
DOI: 10.1016/j.febslet.2005.11.053
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