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Human IgG3 with extended half-life does not improve Fc-gamma receptor-mediated cancer antibody therapies in mice.
Braster, Rens; Grewal, Simran; Visser, Remco; Einarsdottir, Helga K; van Egmond, Marjolein; Vidarsson, Gestur; Bögels, Marijn.
Afiliación
  • Braster R; Department of Molecular Cell Biology and Immunology, VU University Medical Centre, Amsterdam, The Netherlands.
  • Grewal S; Department of Molecular Cell Biology and Immunology, VU University Medical Centre, Amsterdam, The Netherlands.
  • Visser R; Department of Surgery, VU University Medical Centre, Amsterdam, The Netherlands.
  • Einarsdottir HK; Department of Experimental Immunohematology, Sanquin Research, and Landsteiner Laboratory, Academic Medical Centre, University of Amsterdam, Amsterdam, The Netherlands.
  • van Egmond M; Department of Experimental Immunohematology, Sanquin Research, and Landsteiner Laboratory, Academic Medical Centre, University of Amsterdam, Amsterdam, The Netherlands.
  • Vidarsson G; Department of Molecular Cell Biology and Immunology, VU University Medical Centre, Amsterdam, The Netherlands.
  • Bögels M; Department of Surgery, VU University Medical Centre, Amsterdam, The Netherlands.
PLoS One ; 12(5): e0177736, 2017.
Article en En | MEDLINE | ID: mdl-28542406
BACKGROUND: Current anti-cancer therapeutic antibodies that are used in the clinic are predominantly humanized or fully human immunoglobulin G1 (IgG1). These antibodies bind with high affinity to the target antigen and are efficient in activating the immune system via IgG Fc receptors and/or complement. In addition to IgG1, three more isotypes are present in humans, of which IgG3 has been found to be superior compared to human IgG1 in inducing antibody dependent cell cytotoxicity (ADCC), phagocytosis or activation of complement in some models. Nonetheless, no therapeutic human IgG3 mAbs have been developed due to the short in vivo half-life of most known IgG3 allotypes. In this manuscript, we compared the efficacy of V-gene matched IgG1 and IgG3 anti-tumour mAb (TA99) in mice, using natural variants of human IgG3 with short- or long half-life, differing only at position 435 with an arginine or histidine, respectively. RESULTS: In vitro human IgG1 and IgG3 did not show any differences in opsonisation ability of B16F10-gp75 mouse melanoma cells. IgG1, however, was superior in inducing phagocytosis of tumour cells by mouse macrophages. Similarly, in a mouse peritoneal metastasis model we did not detect an improved effect of IgG3 in preventing tumour outgrowth. Moreover, replacing the arginine at position 435 for a histidine in IgG3 to enhance half-life did not result in better suppression of tumour outgrowth compared to wild type IgG3 when injected prior to tumour cell injection. CONCLUSION: In conclusion, human IgG3 does not have improved therapeutic efficacy compared to human IgG1 in a mouse tumour model.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Neoplasias Peritoneales / Melanoma Experimental / Inmunoglobulina G / Monocitos / Receptores de IgG / Anticuerpos Monoclonales Límite: Animals / Humans / Male Idioma: En Revista: PLoS One Asunto de la revista: CIENCIA / MEDICINA Año: 2017 Tipo del documento: Article País de afiliación: Países Bajos Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Neoplasias Peritoneales / Melanoma Experimental / Inmunoglobulina G / Monocitos / Receptores de IgG / Anticuerpos Monoclonales Límite: Animals / Humans / Male Idioma: En Revista: PLoS One Asunto de la revista: CIENCIA / MEDICINA Año: 2017 Tipo del documento: Article País de afiliación: Países Bajos Pais de publicación: Estados Unidos