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Common antigenicity for two glycosidases
Author(s) -
Kakavanos Revecca,
Lehn Pierre,
Callebaut Isabelle,
Meikle Peter J.,
Parkinson-Lawrence Emma J.,
Hopwood John J.,
Brooks Doug A.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.11.053
Subject(s) - antigenicity , epitope , polyclonal antibodies , enzyme replacement therapy , chemistry , monoclonal antibody , antigen , antibody , biochemistry , epitope mapping , mucopolysaccharidosis i , microbiology and biotechnology , biology , immunology , medicine , disease
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, α‐glucosidase (Pompe disease or glycogen storage disease type II, GSD II), and α‐ l ‐iduronidase (Hurler syndrome, mucopolysaccharidosis type I, MPS I). The linear sequence epitope reactivity of affinity purified polyclonal antibodies to recombinant human α‐glucosidase and α‐ 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 α‐glucosidase showed cross‐reactivity with a catalytic structural element of α‐ l ‐iduronidase. In a previous study, in MPS I patients who developed an immune response to ERT, this same site on α‐ 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.