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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- mix :
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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Brooks</name><affiliation wicri:level="1"><hal:affiliation type="laboratory" xml:id="struct-12968" status="INCOMING"> <orgName>Lysosomal Diseases Research Unit, Department of Genetic Medicine, Children Youth and Women's Health Service</orgName> <desc> <address> <addrLine>72 King William Road, North Adelaide, Adelaide, SA 5006, Australia</addrLine> <country key="AU"></country> </address> </desc> <listRelation> <relation active="#struct-305773" type="direct"></relation> </listRelation><tutelles><tutelle active="#struct-305773" type="direct"><org type="institution" xml:id="struct-305773" status="INCOMING"> <orgName>Lysosomal Diseases Research Unit</orgName> <desc> <address> <country key="FR"></country> </address> </desc></org></tutelle></tutelles></hal:affiliation><country>Australie</country></affiliation></author></analytic><idno type="DOI">10.1016/j.febslet.2005.11.053</idno><series><title level="j">FEBS Letters</title><idno type="ISSN">1873-3468</idno><imprint><date type="datePub">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="mix" xml:lang="en"><term>Antibody cross-reactivity</term><term>Antigenicity</term><term>Enzyme replacement therapy</term><term>Epitope reactivity</term><term>Glycosidase</term><term>Lysosomal storage disorders</term></keywords></textClass></profileDesc></teiHeader><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></front></TEI><hal api="V3"> <titleStmt> <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> <editor role="depositor"> <persName> <forename>Sylvia</forename> <surname>Deplanque</surname> </persName> <email type="md5">d65547482aca411120cb7fa8701b584a</email> <email type="domain">impmc.jussieu.fr</email> </editor> </titleStmt> <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> </persName> <email type="md5">d65547482aca411120cb7fa8701b584a</email> <email type="domain">impmc.jussieu.fr</email> </name> </respStmt> </editionStmt> <publicationStmt> <distributor>CCSD</distributor> <idno type="halId">hal-00022577</idno> <idno type="halUri">https://hal.archives-ouvertes.fr/hal-00022577</idno> <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> </seriesStmt> <notesStmt> <note type="audience" n="1">Not set</note> <note type="popular" n="0">No</note> <note type="peer" n="1">Yes</note> </notesStmt> <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> </profileDesc> </hal></record>Pour manipuler ce document sous Unix (Dilib)
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