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Antigen binding by conformational selection in near-germline antibodies.
Blackler, Ryan J; Müller-Loennies, Sven; Pokorny-Lehrer, Barbara; Legg, Max S G; Brade, Lore; Brade, Helmut; Kosma, Paul; Evans, Stephen V.
Afiliación
  • Blackler RJ; Department of Biochemistry and Microbiology, University of Victoria, Victoria British Columbia, Canada.
  • Müller-Loennies S; Research Center Borstel, Leibniz Lung Center, Borstel, Germany.
  • Pokorny-Lehrer B; Department of Chemistry, University of Natural Resources and Life Sciences, Vienna, Austria.
  • Legg MSG; Department of Biochemistry and Microbiology, University of Victoria, Victoria British Columbia, Canada.
  • Brade L; Research Center Borstel, Leibniz Lung Center, Borstel, Germany.
  • Brade H; Research Center Borstel, Leibniz Lung Center, Borstel, Germany.
  • Kosma P; Department of Chemistry, University of Natural Resources and Life Sciences, Vienna, Austria.
  • Evans SV; Department of Biochemistry and Microbiology, University of Victoria, Victoria British Columbia, Canada. Electronic address: svevans@uvic.ca.
J Biol Chem ; 298(5): 101901, 2022 05.
Article en En | MEDLINE | ID: mdl-35395245
Conformational flexibility in antibody-combining sites has been hypothesized to facilitate polyspecificity toward multiple unique epitopes and enable the limited germline repertoire to match an overwhelming diversity of potential antigens; however, elucidating the mechanisms of antigen recognition by flexible antibodies has been understandably challenging. Here, multiple liganded and unliganded crystal structures of the near-germline anticarbohydrate antibodies S25-2 and S25-39 are reported, which reveal an unprecedented diversity of complementarity-determining region H3 conformations in apparent equilibrium. These structures demonstrate that at least some germline or near-germline antibodies are flexible entities sensitive to their chemical environments, with conformational selection available as an evolved mechanism that preserves the inherited ability to recognize common pathogens while remaining adaptable to new threats.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Regiones Determinantes de Complementariedad / Anticuerpos Idioma: En Revista: J Biol Chem Año: 2022 Tipo del documento: Article País de afiliación: Canadá Pais de publicación: Estados Unidos
Texto completo
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Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Regiones Determinantes de Complementariedad / Anticuerpos Idioma: En Revista: J Biol Chem Año: 2022 Tipo del documento: Article País de afiliación: Canadá Pais de publicación: Estados Unidos