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The epitope recognized by rituximab

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The epitope recognized by rituximab. / Binder, Mascha; Otto, Florian; Mertelsmann, Roland; Veelken, Hendrik; Trepel, Martin.

in: BLOOD, Jahrgang 108, Nr. 6, 15.09.2006, S. 1975-8.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Binder, M, Otto, F, Mertelsmann, R, Veelken, H & Trepel, M 2006, 'The epitope recognized by rituximab', BLOOD, Jg. 108, Nr. 6, S. 1975-8. https://doi.org/10.1182/blood-2006-04-014639

APA

Binder, M., Otto, F., Mertelsmann, R., Veelken, H., & Trepel, M. (2006). The epitope recognized by rituximab. BLOOD, 108(6), 1975-8. https://doi.org/10.1182/blood-2006-04-014639

Vancouver

Binder M, Otto F, Mertelsmann R, Veelken H, Trepel M. The epitope recognized by rituximab. BLOOD. 2006 Sep 15;108(6):1975-8. https://doi.org/10.1182/blood-2006-04-014639

Bibtex

@article{c3a7cbae309d436e8d660c087b80c152,
title = "The epitope recognized by rituximab",
abstract = "Rituximab is a monoclonal antibody widely used in the treatment of malignant lymphoma and autoimmunity. Its epitope within the B-cell antigen CD20 is largely unknown. We used phage display libraries to select peptides binding to rituximab. Enriched peptides showed 2 sequence patterns: one motif (CALMIANSC) is related to (170)ANPS(173) within CD20, while another motif (WEWTI) may mimic the CD20 segment (182)YCYSI(185). Phages displaying either motif specifically bound rituximab. Binding to rituximab by the CD20 peptides ANPS and YCYSI was weak when used separately and enhanced when both peptides were linked. Recombinant CD20 extracellular loop proteins blocked binding of the selected CWWEWTIGC phage to rituximab, suggesting that CWWEWTIGC mimics the epitope. Blocking capacity was strongly reduced upon mutation of the CD20 strings ANPS or YCYSI. We conclude that rituximab binds a discontinuous epitope in CD20, comprised of (170)ANPS(173) and (182)YCYSI(185), with both strings brought in steric proximity by a disulfide bridge between C(167) and C(183).",
keywords = "Amino Acid Sequence, Antibodies, Monoclonal, Antibodies, Monoclonal, Murine-Derived, Antigens, CD20, B-Lymphocytes, Binding Sites, Epitopes, Humans, In Vitro Techniques, Molecular Sequence Data, Peptide Library, Protein Structure, Tertiary, Recombinant Fusion Proteins, Rituximab, Journal Article, Research Support, Non-U.S. Gov't",
author = "Mascha Binder and Florian Otto and Roland Mertelsmann and Hendrik Veelken and Martin Trepel",
year = "2006",
month = sep,
day = "15",
doi = "10.1182/blood-2006-04-014639",
language = "English",
volume = "108",
pages = "1975--8",
journal = "BLOOD",
issn = "0006-4971",
publisher = "American Society of Hematology",
number = "6",

}

RIS

TY - JOUR

T1 - The epitope recognized by rituximab

AU - Binder, Mascha

AU - Otto, Florian

AU - Mertelsmann, Roland

AU - Veelken, Hendrik

AU - Trepel, Martin

PY - 2006/9/15

Y1 - 2006/9/15

N2 - Rituximab is a monoclonal antibody widely used in the treatment of malignant lymphoma and autoimmunity. Its epitope within the B-cell antigen CD20 is largely unknown. We used phage display libraries to select peptides binding to rituximab. Enriched peptides showed 2 sequence patterns: one motif (CALMIANSC) is related to (170)ANPS(173) within CD20, while another motif (WEWTI) may mimic the CD20 segment (182)YCYSI(185). Phages displaying either motif specifically bound rituximab. Binding to rituximab by the CD20 peptides ANPS and YCYSI was weak when used separately and enhanced when both peptides were linked. Recombinant CD20 extracellular loop proteins blocked binding of the selected CWWEWTIGC phage to rituximab, suggesting that CWWEWTIGC mimics the epitope. Blocking capacity was strongly reduced upon mutation of the CD20 strings ANPS or YCYSI. We conclude that rituximab binds a discontinuous epitope in CD20, comprised of (170)ANPS(173) and (182)YCYSI(185), with both strings brought in steric proximity by a disulfide bridge between C(167) and C(183).

AB - Rituximab is a monoclonal antibody widely used in the treatment of malignant lymphoma and autoimmunity. Its epitope within the B-cell antigen CD20 is largely unknown. We used phage display libraries to select peptides binding to rituximab. Enriched peptides showed 2 sequence patterns: one motif (CALMIANSC) is related to (170)ANPS(173) within CD20, while another motif (WEWTI) may mimic the CD20 segment (182)YCYSI(185). Phages displaying either motif specifically bound rituximab. Binding to rituximab by the CD20 peptides ANPS and YCYSI was weak when used separately and enhanced when both peptides were linked. Recombinant CD20 extracellular loop proteins blocked binding of the selected CWWEWTIGC phage to rituximab, suggesting that CWWEWTIGC mimics the epitope. Blocking capacity was strongly reduced upon mutation of the CD20 strings ANPS or YCYSI. We conclude that rituximab binds a discontinuous epitope in CD20, comprised of (170)ANPS(173) and (182)YCYSI(185), with both strings brought in steric proximity by a disulfide bridge between C(167) and C(183).

KW - Amino Acid Sequence

KW - Antibodies, Monoclonal

KW - Antibodies, Monoclonal, Murine-Derived

KW - Antigens, CD20

KW - B-Lymphocytes

KW - Binding Sites

KW - Epitopes

KW - Humans

KW - In Vitro Techniques

KW - Molecular Sequence Data

KW - Peptide Library

KW - Protein Structure, Tertiary

KW - Recombinant Fusion Proteins

KW - Rituximab

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1182/blood-2006-04-014639

DO - 10.1182/blood-2006-04-014639

M3 - SCORING: Journal article

C2 - 16705086

VL - 108

SP - 1975

EP - 1978

JO - BLOOD

JF - BLOOD

SN - 0006-4971

IS - 6

ER -