B-Cell and T-Cell Epitopes in Anti-factor VIII Immune Responses
Identifieur interne : 002322 ( Istex/Corpus ); précédent : 002321; suivant : 002323B-Cell and T-Cell Epitopes in Anti-factor VIII Immune Responses
Auteurs : Kathleen P. Pratt ; Arthur R. ThompsonSource :
- Clinical Reviews in Allergy & Immunology [ 1080-0549 ] ; 2009-10-01.
English descriptors
Abstract
Abstract: Adequate hemostasis is achieved for many hemophilia A patients by infusion of plasma-derived or recombinant factor VIII (FVIII), but unfortunately, a significant subset of patients develop an immune response in which anti-FVIII antibodies, referred to clinically as “inhibitors,” interfere with its procoagulant activity. Inhibitors are the subset of anti-FVIII antibodies that bind to surfaces on FVIII (B-cell epitopes) that are important for its proper functioning in coagulation. Less antigenic FVIII molecules may be designed by identifying and then modifying the amino acid sequences of inhibitor B-cell epitopes. Conversely, characterization of these epitopes can yield important information regarding functionally important surfaces on FVIII. The production of inhibitor antibodies is driven by T cells. T cells recognize FVIII as foreign when FVIII-derived peptides bind to major histocompatibility complex (MHC) class II molecules on the surface of antigen-presenting cells. The class II–peptide complexes must then be recognized by T-cell receptors (TCRs). T-cell stimulation requires sustained association of antigen-presenting cells and T cells through formation of a class II–peptide–TCR complex, and peptide sequences that mediate this association are termed “T-cell epitopes.” MHC class II tetramers that bind FVIII-derived peptides and recognize antigen-specific TCRs are proving useful in the characterization of human leukocyte antigen-restricted T-cell responses to FVIII.
Url:
DOI: 10.1007/s12016-009-8120-7
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<front><div type="abstract" xml:lang="en">Abstract: Adequate hemostasis is achieved for many hemophilia A patients by infusion of plasma-derived or recombinant factor VIII (FVIII), but unfortunately, a significant subset of patients develop an immune response in which anti-FVIII antibodies, referred to clinically as “inhibitors,” interfere with its procoagulant activity. Inhibitors are the subset of anti-FVIII antibodies that bind to surfaces on FVIII (B-cell epitopes) that are important for its proper functioning in coagulation. Less antigenic FVIII molecules may be designed by identifying and then modifying the amino acid sequences of inhibitor B-cell epitopes. Conversely, characterization of these epitopes can yield important information regarding functionally important surfaces on FVIII. The production of inhibitor antibodies is driven by T cells. T cells recognize FVIII as foreign when FVIII-derived peptides bind to major histocompatibility complex (MHC) class II molecules on the surface of antigen-presenting cells. The class II–peptide complexes must then be recognized by T-cell receptors (TCRs). T-cell stimulation requires sustained association of antigen-presenting cells and T cells through formation of a class II–peptide–TCR complex, and peptide sequences that mediate this association are termed “T-cell epitopes.” MHC class II tetramers that bind FVIII-derived peptides and recognize antigen-specific TCRs are proving useful in the characterization of human leukocyte antigen-restricted T-cell responses to FVIII.</div>
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<Para>Adequate hemostasis is achieved for many hemophilia A patients by infusion of plasma-derived or recombinant factor VIII (FVIII), but unfortunately, a significant subset of patients develop an immune response in which anti-FVIII antibodies, referred to clinically as “inhibitors,” interfere with its procoagulant activity. Inhibitors are the subset of anti-FVIII antibodies that bind to surfaces on FVIII (B-cell epitopes) that are important for its proper functioning in coagulation. Less antigenic FVIII molecules may be designed by identifying and then modifying the amino acid sequences of inhibitor B-cell epitopes. Conversely, characterization of these epitopes can yield important information regarding functionally important surfaces on FVIII. The production of inhibitor antibodies is driven by T cells. T cells recognize FVIII as foreign when FVIII-derived peptides bind to major histocompatibility complex (MHC) class II molecules on the surface of antigen-presenting cells. The class II–peptide complexes must then be recognized by T-cell receptors (TCRs). T-cell stimulation requires sustained association of antigen-presenting cells and T cells through formation of a class II–peptide–TCR complex, and peptide sequences that mediate this association are termed “T-cell epitopes.” MHC class II tetramers that bind FVIII-derived peptides and recognize antigen-specific TCRs are proving useful in the characterization of human leukocyte antigen-restricted T-cell responses to FVIII.</Para>
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<abstract lang="en">Abstract: Adequate hemostasis is achieved for many hemophilia A patients by infusion of plasma-derived or recombinant factor VIII (FVIII), but unfortunately, a significant subset of patients develop an immune response in which anti-FVIII antibodies, referred to clinically as “inhibitors,” interfere with its procoagulant activity. Inhibitors are the subset of anti-FVIII antibodies that bind to surfaces on FVIII (B-cell epitopes) that are important for its proper functioning in coagulation. Less antigenic FVIII molecules may be designed by identifying and then modifying the amino acid sequences of inhibitor B-cell epitopes. Conversely, characterization of these epitopes can yield important information regarding functionally important surfaces on FVIII. The production of inhibitor antibodies is driven by T cells. T cells recognize FVIII as foreign when FVIII-derived peptides bind to major histocompatibility complex (MHC) class II molecules on the surface of antigen-presenting cells. The class II–peptide complexes must then be recognized by T-cell receptors (TCRs). T-cell stimulation requires sustained association of antigen-presenting cells and T cells through formation of a class II–peptide–TCR complex, and peptide sequences that mediate this association are termed “T-cell epitopes.” MHC class II tetramers that bind FVIII-derived peptides and recognize antigen-specific TCRs are proving useful in the characterization of human leukocyte antigen-restricted T-cell responses to FVIII.</abstract>
<subject lang="en"><genre>Keywords</genre>
<topic>Hemophilia A</topic>
<topic>Inhibitory antibody</topic>
<topic>B-cell epitopes</topic>
<topic>T-cell immune responses</topic>
</subject>
<relatedItem type="host"><titleInfo><title>Clinical Reviews in Allergy & Immunology</title>
</titleInfo>
<titleInfo type="abbreviated"><title>Clinic Rev Allerg Immunol</title>
</titleInfo>
<genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre>
<originInfo><publisher>Springer</publisher>
<dateIssued encoding="w3cdtf">2009-09-11</dateIssued>
<copyrightDate encoding="w3cdtf">2009</copyrightDate>
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<subject><genre>Medicine & Public Health</genre>
<topic>Internal Medicine</topic>
<topic>Immunology</topic>
<topic>Allergology</topic>
</subject>
<identifier type="ISSN">1080-0549</identifier>
<identifier type="eISSN">1559-0267</identifier>
<identifier type="JournalID">12016</identifier>
<identifier type="IssueArticleCount">9</identifier>
<identifier type="VolumeIssueCount">3</identifier>
<part><date>2009</date>
<detail type="issue"><title>Anti-Factor VIII Antibodies (Inhibitors) in Hemophilia; Guest Editor: Svini V. Kaveri</title>
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<detail type="volume"><number>37</number>
<caption>vol.</caption>
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<detail type="issue"><number>2</number>
<caption>no.</caption>
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<extent unit="pages"><start>80</start>
<end>95</end>
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</part>
<recordInfo><recordOrigin>Humana Press Inc., 2009</recordOrigin>
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<identifier type="ark">ark:/67375/VQC-H00V6SSC-K</identifier>
<identifier type="DOI">10.1007/s12016-009-8120-7</identifier>
<identifier type="ArticleID">8120</identifier>
<identifier type="ArticleID">s12016-009-8120-7</identifier>
<accessCondition type="use and reproduction" contentType="copyright">Humana Press Inc., 2009</accessCondition>
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