Basic immunological aspects of botulinum toxin therapy.
Identifieur interne : 003509 ( PubMed/Corpus ); précédent : 003508; suivant : 003510Basic immunological aspects of botulinum toxin therapy.
Auteurs : M Zouhair AtassiSource :
- Movement disorders : official journal of the Movement Disorder Society [ 0885-3185 ] ; 2004.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Antibodies (immunology), Botulinum Toxins (immunology), Botulinum Toxins (therapeutic use), Cross Reactions, Epitope Mapping, Humans, Immunization (methods), Immunotherapy, Neurotoxins (immunology), Neurotoxins (therapeutic use), Peptide Fragments (chemistry), Peptide Fragments (immunology), Tetanus Toxin (immunology), Time Factors.
- MESH :
- chemical , chemistry : Peptide Fragments.
- chemical , immunology : Antibodies, Botulinum Toxins, Neurotoxins, Peptide Fragments, Tetanus Toxin.
- chemical , therapeutic use : Botulinum Toxins, Neurotoxins.
- methods : Immunization.
- Amino Acid Sequence, Animals, Cross Reactions, Epitope Mapping, Humans, Immunotherapy, Time Factors.
Abstract
Previous studies in this laboratory had mapped the immune recognition profile of the regions recognized antibodies (Abs) and by T cells on the protective H(C) domain (C-terminal fragment corresponding to residues 855-1296 of the heavy chain) of botulinum neurotoxin serotype A (BoNT/A). The localization of these regions has several potential applications and has provided a basis for the understanding of immunoresistance to treatment. We briefly outline these localized regions and discuss the impact of these findings on the immunotherapeutic applications of BoNT/A. Immunoresistance to toxin therapy can appear in some patients after a few injections with the toxin. Our epitope mapping studies have shown that several factors can influence the immune response to the toxin. These factors include dose, duration of treatment, frequency of immunization, and quality of the toxin. The immune response to the whole toxin is under genetic control, and the response to each epitope is under separate genetic control. Therefore, the appearance of blocking Abs (i.e., immunoresistance) in patients might be controlled by the major histocompatability of the host. Once a patient becomes immunoresistant to one toxin then switching to another toxin will most often be of limited and short-lived benefit, because the patient becomes rapidly immunoresistant to the second toxin. Finally, because of the considerable structural homology between tetanus neurotoxin (TeNT) and BoNTs, it is possible, although not certain, that a prior active immune response to TeNT might play some role in the early appearance on anti-BoNT Abs in some patients.
DOI: 10.1002/mds.20020
PubMed: 15027058
Links to Exploration step
pubmed:15027058Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Basic immunological aspects of botulinum toxin therapy.</title>
<author><name sortKey="Atassi, M Zouhair" sort="Atassi, M Zouhair" uniqKey="Atassi M" first="M Zouhair" last="Atassi">M Zouhair Atassi</name>
<affiliation><nlm:affiliation>Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas 77030, USA. matassi@bcm.tmc.edu</nlm:affiliation>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2004">2004</date>
<idno type="RBID">pubmed:15027058</idno>
<idno type="pmid">15027058</idno>
<idno type="doi">10.1002/mds.20020</idno>
<idno type="wicri:Area/PubMed/Corpus">003509</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Basic immunological aspects of botulinum toxin therapy.</title>
<author><name sortKey="Atassi, M Zouhair" sort="Atassi, M Zouhair" uniqKey="Atassi M" first="M Zouhair" last="Atassi">M Zouhair Atassi</name>
<affiliation><nlm:affiliation>Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas 77030, USA. matassi@bcm.tmc.edu</nlm:affiliation>
</affiliation>
</author>
</analytic>
<series><title level="j">Movement disorders : official journal of the Movement Disorder Society</title>
<idno type="ISSN">0885-3185</idno>
<imprint><date when="2004" type="published">2004</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Antibodies (immunology)</term>
<term>Botulinum Toxins (immunology)</term>
<term>Botulinum Toxins (therapeutic use)</term>
<term>Cross Reactions</term>
<term>Epitope Mapping</term>
<term>Humans</term>
<term>Immunization (methods)</term>
<term>Immunotherapy</term>
<term>Neurotoxins (immunology)</term>
<term>Neurotoxins (therapeutic use)</term>
<term>Peptide Fragments (chemistry)</term>
<term>Peptide Fragments (immunology)</term>
<term>Tetanus Toxin (immunology)</term>
<term>Time Factors</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peptide Fragments</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies</term>
<term>Botulinum Toxins</term>
<term>Neurotoxins</term>
<term>Peptide Fragments</term>
<term>Tetanus Toxin</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="therapeutic use" xml:lang="en"><term>Botulinum Toxins</term>
<term>Neurotoxins</term>
</keywords>
<keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Immunization</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Cross Reactions</term>
<term>Epitope Mapping</term>
<term>Humans</term>
<term>Immunotherapy</term>
<term>Time Factors</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Previous studies in this laboratory had mapped the immune recognition profile of the regions recognized antibodies (Abs) and by T cells on the protective H(C) domain (C-terminal fragment corresponding to residues 855-1296 of the heavy chain) of botulinum neurotoxin serotype A (BoNT/A). The localization of these regions has several potential applications and has provided a basis for the understanding of immunoresistance to treatment. We briefly outline these localized regions and discuss the impact of these findings on the immunotherapeutic applications of BoNT/A. Immunoresistance to toxin therapy can appear in some patients after a few injections with the toxin. Our epitope mapping studies have shown that several factors can influence the immune response to the toxin. These factors include dose, duration of treatment, frequency of immunization, and quality of the toxin. The immune response to the whole toxin is under genetic control, and the response to each epitope is under separate genetic control. Therefore, the appearance of blocking Abs (i.e., immunoresistance) in patients might be controlled by the major histocompatability of the host. Once a patient becomes immunoresistant to one toxin then switching to another toxin will most often be of limited and short-lived benefit, because the patient becomes rapidly immunoresistant to the second toxin. Finally, because of the considerable structural homology between tetanus neurotoxin (TeNT) and BoNTs, it is possible, although not certain, that a prior active immune response to TeNT might play some role in the early appearance on anti-BoNT Abs in some patients.</div>
</front>
</TEI>
<pubmed><MedlineCitation Owner="NLM" Status="MEDLINE"><PMID Version="1">15027058</PMID>
<DateCreated><Year>2004</Year>
<Month>03</Month>
<Day>17</Day>
</DateCreated>
<DateCompleted><Year>2004</Year>
<Month>06</Month>
<Day>15</Day>
</DateCompleted>
<DateRevised><Year>2010</Year>
<Month>11</Month>
<Day>18</Day>
</DateRevised>
<Article PubModel="Print"><Journal><ISSN IssnType="Print">0885-3185</ISSN>
<JournalIssue CitedMedium="Print"><Volume>19 Suppl 8</Volume>
<PubDate><Year>2004</Year>
<Month>Mar</Month>
</PubDate>
</JournalIssue>
<Title>Movement disorders : official journal of the Movement Disorder Society</Title>
<ISOAbbreviation>Mov. Disord.</ISOAbbreviation>
</Journal>
<ArticleTitle>Basic immunological aspects of botulinum toxin therapy.</ArticleTitle>
<Pagination><MedlinePgn>S68-84</MedlinePgn>
</Pagination>
<Abstract><AbstractText>Previous studies in this laboratory had mapped the immune recognition profile of the regions recognized antibodies (Abs) and by T cells on the protective H(C) domain (C-terminal fragment corresponding to residues 855-1296 of the heavy chain) of botulinum neurotoxin serotype A (BoNT/A). The localization of these regions has several potential applications and has provided a basis for the understanding of immunoresistance to treatment. We briefly outline these localized regions and discuss the impact of these findings on the immunotherapeutic applications of BoNT/A. Immunoresistance to toxin therapy can appear in some patients after a few injections with the toxin. Our epitope mapping studies have shown that several factors can influence the immune response to the toxin. These factors include dose, duration of treatment, frequency of immunization, and quality of the toxin. The immune response to the whole toxin is under genetic control, and the response to each epitope is under separate genetic control. Therefore, the appearance of blocking Abs (i.e., immunoresistance) in patients might be controlled by the major histocompatability of the host. Once a patient becomes immunoresistant to one toxin then switching to another toxin will most often be of limited and short-lived benefit, because the patient becomes rapidly immunoresistant to the second toxin. Finally, because of the considerable structural homology between tetanus neurotoxin (TeNT) and BoNTs, it is possible, although not certain, that a prior active immune response to TeNT might play some role in the early appearance on anti-BoNT Abs in some patients.</AbstractText>
<CopyrightInformation>Copyright 2004 Movement Disorder Society</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Atassi</LastName>
<ForeName>M Zouhair</ForeName>
<Initials>MZ</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas 77030, USA. matassi@bcm.tmc.edu</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
<PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType>
<PublicationType UI="D016454">Review</PublicationType>
</PublicationTypeList>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Mov Disord</MedlineTA>
<NlmUniqueID>8610688</NlmUniqueID>
<ISSNLinking>0885-3185</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000906">Antibodies</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D009498">Neurotoxins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D010446">Peptide Fragments</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D013744">Tetanus Toxin</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.4.24.69</RegistryNumber>
<NameOfSubstance UI="D001905">Botulinum Toxins</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName MajorTopicYN="N" UI="D000595">Amino Acid Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName MajorTopicYN="N" UI="D000818">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName MajorTopicYN="N" UI="D000906">Antibodies</DescriptorName>
<QualifierName MajorTopicYN="Y" UI="Q000276">immunology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName MajorTopicYN="N" UI="D001905">Botulinum Toxins</DescriptorName>
<QualifierName MajorTopicYN="Y" UI="Q000276">immunology</QualifierName>
<QualifierName MajorTopicYN="N" UI="Q000627">therapeutic use</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName MajorTopicYN="N" UI="D003429">Cross Reactions</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName MajorTopicYN="N" UI="D018604">Epitope Mapping</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName MajorTopicYN="N" UI="D006801">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName MajorTopicYN="N" UI="D007114">Immunization</DescriptorName>
<QualifierName MajorTopicYN="N" UI="Q000379">methods</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName MajorTopicYN="Y" UI="D007167">Immunotherapy</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName MajorTopicYN="N" UI="D009498">Neurotoxins</DescriptorName>
<QualifierName MajorTopicYN="Y" UI="Q000276">immunology</QualifierName>
<QualifierName MajorTopicYN="N" UI="Q000627">therapeutic use</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName MajorTopicYN="N" UI="D010446">Peptide Fragments</DescriptorName>
<QualifierName MajorTopicYN="N" UI="Q000737">chemistry</QualifierName>
<QualifierName MajorTopicYN="N" UI="Q000276">immunology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName MajorTopicYN="N" UI="D013744">Tetanus Toxin</DescriptorName>
<QualifierName MajorTopicYN="N" UI="Q000276">immunology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName MajorTopicYN="N" UI="D013997">Time Factors</DescriptorName>
</MeshHeading>
</MeshHeadingList>
<NumberOfReferences>157</NumberOfReferences>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2004</Year>
<Month>3</Month>
<Day>18</Day>
<Hour>5</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2004</Year>
<Month>6</Month>
<Day>16</Day>
<Hour>5</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2004</Year>
<Month>3</Month>
<Day>18</Day>
<Hour>5</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">15027058</ArticleId>
<ArticleId IdType="doi">10.1002/mds.20020</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Santé/explor/MovDisordV3/Data/PubMed/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 003509 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd -nk 003509 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Wicri/Santé |area= MovDisordV3 |flux= PubMed |étape= Corpus |type= RBID |clé= pubmed:15027058 |texte= Basic immunological aspects of botulinum toxin therapy. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/RBID.i -Sk "pubmed:15027058" \ | HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd \ | NlmPubMed2Wicri -a MovDisordV3
![]() | This area was generated with Dilib version V0.6.23. | ![]() |