Common antigenicity for two glycosidases.
Identifieur interne : 000194 ( Hal/Curation ); précédent : 000193; suivant : 000195Common antigenicity for two glycosidases.
Auteurs : Revecca Kakavanos [Australie] ; Pierre Lehn [France] ; Isabelle Callebaut [France] ; Peter J. Meiklea [Australie] ; Emma J. Parkinson-Lawrence [Australie] ; John J. Hopwood [Australie] ; Doug A. Brooks [Australie]Source :
- FEBS Letters [ 1873-3468 ] ; 2006.
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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, 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.
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DOI: 10.1016/j.febslet.2005.11.053
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<front><div type="abstract" xml:lang="en">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.</div>
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</author>
<author role="aut"> <persName> <forename type="first">Emma J.</forename>
<surname>Parkinson-Lawrence</surname>
</persName>
<idno type="halauthorid">91086</idno>
<affiliation ref="#struct-12968"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">John J.</forename>
<surname>Hopwood</surname>
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<idno type="halauthorid">91087</idno>
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</author>
<author role="aut"> <persName> <forename type="first">Doug A.</forename>
<surname>Brooks</surname>
</persName>
<idno type="halauthorid">91088</idno>
<affiliation ref="#struct-12968"></affiliation>
<affiliation ref="#struct-12969"></affiliation>
</author>
<editor role="depositor"> <persName> <forename>Sylvia</forename>
<surname>Deplanque</surname>
</persName>
<email type="md5">d65547482aca411120cb7fa8701b584a</email>
<email type="domain">impmc.jussieu.fr</email>
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<editionStmt> <edition n="v1" type="current"> <date type="whenSubmitted">2006-04-11 14:38:05</date>
<date type="whenModified">2016-10-12 01:04:23</date>
<date type="whenReleased">2006-04-11 14:38:05</date>
<date type="whenProduced">2006</date>
</edition>
<respStmt> <resp>contributor</resp>
<name key="103676"> <persName> <forename>Sylvia</forename>
<surname>Deplanque</surname>
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<email type="md5">d65547482aca411120cb7fa8701b584a</email>
<email type="domain">impmc.jussieu.fr</email>
</name>
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<idno type="halId">hal-00022577</idno>
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<idno type="halBibtex">kakavanos:hal-00022577</idno>
<idno type="halRefHtml">FEBS Letters, Wiley, 2006, 580, pp.87-92. <10.1016/j.febslet.2005.11.053></idno>
<idno type="halRef">FEBS Letters, Wiley, 2006, 580, pp.87-92. <10.1016/j.febslet.2005.11.053></idno>
</publicationStmt>
<seriesStmt> <idno type="stamp" n="IMPMC" p="UPMC">Institut de Minéralogie, de Physique des Matériaux et de Cosmochimie</idno>
<idno type="stamp" n="ALLINSP">Tout INSP</idno>
<idno type="stamp" n="UNIV-BREST">Université de Bretagne occidentale - Brest</idno>
<idno type="stamp" n="CNRS">CNRS - Centre national de la recherche scientifique</idno>
<idno type="stamp" n="UNIV-PARIS7">Université Denis Diderot - Paris VII</idno>
<idno type="stamp" n="UPMC">Université Pierre et Marie Curie</idno>
<idno type="stamp" n="USPC">Université Sorbonne Paris Cité</idno>
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<notesStmt> <note type="audience" n="1">Not set</note>
<note type="popular" n="0">No</note>
<note type="peer" n="1">Yes</note>
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<sourceDesc> <biblStruct> <analytic> <title xml:lang="en">Common antigenicity for two glycosidases.</title>
<author role="aut"> <persName> <forename type="first">Revecca</forename>
<surname>Kakavanos</surname>
</persName>
<idno type="halauthorid">91083</idno>
<affiliation ref="#struct-12968"></affiliation>
<affiliation ref="#struct-12969"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Pierre</forename>
<surname>Lehn</surname>
</persName>
<idno type="halauthorid">91084</idno>
<affiliation ref="#struct-2971"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Isabelle</forename>
<surname>Callebaut</surname>
</persName>
<idno type="halauthorid">85819</idno>
<affiliation ref="#struct-3204"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Peter J.</forename>
<surname>Meiklea</surname>
</persName>
<idno type="halauthorid">91085</idno>
<affiliation ref="#struct-12968"></affiliation>
<affiliation ref="#struct-12969"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Emma J.</forename>
<surname>Parkinson-Lawrence</surname>
</persName>
<idno type="halauthorid">91086</idno>
<affiliation ref="#struct-12968"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">John J.</forename>
<surname>Hopwood</surname>
</persName>
<idno type="halauthorid">91087</idno>
<affiliation ref="#struct-12968"></affiliation>
<affiliation ref="#struct-12969"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Doug A.</forename>
<surname>Brooks</surname>
</persName>
<idno type="halauthorid">91088</idno>
<affiliation ref="#struct-12968"></affiliation>
<affiliation ref="#struct-12969"></affiliation>
</author>
</analytic>
<monogr> <idno type="halJournalId" status="VALID">13319</idno>
<idno type="issn">1873-3468</idno>
<title level="j">FEBS Letters</title>
<imprint> <publisher>Wiley</publisher>
<biblScope unit="volume">580</biblScope>
<biblScope unit="pp">87-92</biblScope>
<date type="datePub">2006</date>
</imprint>
</monogr>
<idno type="doi">10.1016/j.febslet.2005.11.053</idno>
</biblStruct>
</sourceDesc>
<profileDesc> <langUsage> <language ident="en">English</language>
</langUsage>
<textClass> <keywords scheme="author"> <term xml:lang="en">Glycosidase</term>
<term xml:lang="en">Antigenicity</term>
<term xml:lang="en">Epitope reactivity</term>
<term xml:lang="en">Antibody cross-reactivity</term>
<term xml:lang="en">Enzyme replacement therapy</term>
<term xml:lang="en">Lysosomal storage disorders</term>
</keywords>
<classCode scheme="halTypology" n="ART">Journal articles</classCode>
</textClass>
<abstract xml:lang="en">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.</abstract>
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