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Home All issues Volume 35 / No 12 (Décembre 2019) Med Sci (Paris), 35 12 (2019) 1098-1105 References
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Issue
Med Sci (Paris)
Volume 35, Number 12, Décembre 2019
Anticorps monoclonaux en thérapeutique
Page(s) 1098 - 1105
Section Les nouveaux formats d’anticorps
DOI https://doi.org/10.1051/medsci/2019218
Published online 06 January 2020
  1. Burton DR , Immunoglobulin G: functional sites. Mol Immunol. 1985;22:161–206. [Google Scholar]
  2. Ugurlar D, Howes SC, de Kreuk BJ, et al., Structures of C1-IgG1 provide insights into how danger pattern recognition activates complement. Science. 2018;359:794–7. [Google Scholar]
  3. Strasser J, De Jong RN, Beurskens FJ, et al., Unraveling the macromolecular pathways of IgG oligomerization and complement activation on antigenic surfaces. Nano Lett. 2019;19:4787–96. [CrossRef] [PubMed] [Google Scholar]
  4. Bindon CI , Human monoclonal IgG isotypes differ in complement activating function at the level of C4 as well as C1q. J Exp Med. 1988;168:127–42. [CrossRef] [PubMed] [Google Scholar]
  5. Morgan A, Jones ND, Nesbitt AM, et al., The N-terminal end of the CH2 domain of chimeric human IgG1 anti-HLA-DR is necessary for C1q, Fc gamma RI and Fc gamma RIII binding. Immunology. 1995;86:319–24. [PubMed] [Google Scholar]
  6. Guddat LW, Herron JN, Edmundson AB , Three-dimensional structure of a human immunoglobulin with a hinge deletion. Proc Natl Acad Sci USA. 1993;90:4271–75. [CrossRef] [Google Scholar]
  7. Saphire EO, Stanfield RL, Max Crispin MD, et al., Contrasting IgG structures reveal extreme asymmetry and flexibility. J Mol Biol. 2002;319:9–18. [Google Scholar]
  8. Roux KH, Strelets L, Michaelsen TE , Flexibility of human IgG subclasses. J Immunol. 1997;159:3372–82. [PubMed] [Google Scholar]
  9. Bruhns P, Iannascoli B, England P, et al., Specificity and affinity of human Fc receptors and their polymorphic variants for human IgG subclasses. Blood. 2009;113:3716–25. [Google Scholar]
  10. Rayner LE, Hui GK, Gor J, et al., The solution structures of two human IgG1 antibodies show conformational stability and accommodate their C1q and FcγR ligands. J Biol Chem. 2015;290:8420–38. [CrossRef] [PubMed] [Google Scholar]
  11. Dillon TM, Ricci MS, Vezina C, et al., Structural and functional characterization of disulfide isoforms of the human IgG2 subclass. J Biol Chem. 2008;283:16206–15. [CrossRef] [PubMed] [Google Scholar]
  12. Rispens T, Ooijevaar-de Heer P, Bende O, et al., Mechanism of immunoglobulin G4 Fab-arm exchange. J Am Chem Soc. 2011;133:10302–11. [Google Scholar]
  13. Labrijn AF, Buijsse AO, van den Bremer ETJ, et al., Therapeutic IgG4 antibodies engage in Fab-arm exchange with endogenous human IgG4 in vivo. Nat Biotechnol. 2009;27:767–71. [CrossRef] [PubMed] [Google Scholar]
  14. Rayner LE, Hui GK, Gor J, et al., The Fab conformations in the solution structure of human immunoglobulin G4 (IgG4) restrict access to its Fc region: Implications for functional activity. J Biol Chem. 2014;289:20740–56. [CrossRef] [PubMed] [Google Scholar]
  15. Bloom JW, Madanat MS, Marriott D, et al., Intrachain disulfide bond in the core hinge region of human IgG4. Protein Sci. 2008;6:407–15. [Google Scholar]
  16. Liu L, Lu J, Allan BW, et al., Generation and characterization of ixekizumab, a humanized monoclonal antibody that neutralizes interleukin-17A. J Inflamm Res. 2016; 9: 39–50. [PubMed] [Google Scholar]
  17. Wyant T, Yang L, Fedyk E , In vitro assessment of the effects of vedolizumab binding on peripheral blood lymphocytes. mAbs. 2013;5:842–50. [CrossRef] [PubMed] [Google Scholar]
  18. Peng L, Oganesyan V, Wu H, et al., Molecular basis for antagonistic activity of anifrolumab, an anti-interferon – α receptor 1 antibody. mAbs. 2015;7:428–39. [CrossRef] [PubMed] [Google Scholar]
  19. Riggs JM, Hanna RN, Rajan B, et al., Characterisation of anifrolumab, a fully human anti-interferon receptor antagonist antibody for the treatment of systemic lupus erythematosus. Lupus Sci Med. 2018;5:e000261. [Google Scholar]
  20. Gonzalez A, Broussas M, Beau-Larvor C, et al., A novel antagonist anti-cMet antibody with antitumor activities targeting both ligand-dependent and ligand-independent c-Met receptors: A full antagonist anti-c-Met MAb with in vivo activity. Int J Cancer. 2016;139:1851–63. [CrossRef] [PubMed] [Google Scholar]
  21. Könitzer JD, Sieron A, Wacker A, et al., Reformatting Rituximab into human IgG2 and IgG4 isotypes dramatically improves apoptosis induction in vitro . PLoS One. 2015;10:e0145633. [CrossRef] [PubMed] [Google Scholar]
  22. Wang Q, Chen Y, Pelletier M, et al., Enhancement of antibody functions through Fc multiplications. mAbs. 2017;9:393–403. [CrossRef] [PubMed] [Google Scholar]
  23. Porter RR , The hydrolysis of rabbit y-globulin and antibodies with crystalline papain. Biochem J. 1959;73:119–26. [CrossRef] [PubMed] [Google Scholar]
  24. Nisonoff A, Wissler FC, Lipman LN , Properties of the major component of a peptic digest of rabbit antibody. Science. 1960;132:1770–1. [Google Scholar]
  25. Brezski RJ, Vafa O, Petrone D, et al., Tumor-associated and microbial proteases compromise host IgG effector functions by a single cleavage proximal to the hinge. Proc Natl Acad Sci USA. 2009;106:17864–69. [CrossRef] [Google Scholar]
  26. Ryan MH, Petrone D, Nemeth JF, et al., Proteolysis of purified IgGs by human and bacterial enzymes in vitro and the detection of specific proteolytic fragments of endogenous IgG in rheumatoid synovial fluid. Mol Immunol. 2008;45:1837–46. [Google Scholar]
  27. Biancheri P, Brezski RJ, Di Sabatino A, et al., Proteolytic cleavage and loss of function of biologic agents that neutralize tumor necrosis factor in the mucosa of patients with inflammatory bowel disease. Gastroenterology. 2015;149:1564–74. [CrossRef] [PubMed] [Google Scholar]
  28. Brezski RJ, Jordan RE , Cleavage of IgGs by proteases associated with invasive diseases. mAbs. 2010;2:212–20. [Google Scholar]
  29. Brezski RJ, Oberholtzer A, Strake B, et al., The in vitro resistance of IgG2 to proteolytic attack concurs with a comparative paucity of autoantibodies against peptide analogs of the IgG2 hinge. mAbs. 2011;3:558–67. [CrossRef] [PubMed] [Google Scholar]
  30. Hsiao HC, Fan X, Jordan RE, et al., Proteolytic single hinge cleavage of pertuzumab impairs its Fc effector function and antitumor activity in vitro and in vivo. Breast Cancer Res. 2018; 20; 20h43.. [Google Scholar]
  31. Fan X, Brezski RJ, Fa M, et al., A single proteolytic cleavage within the lower hinge of trastuzumab reduces immune effector function and in vivo efficacy. Breast Cancer Res. 2012;14:R116. [CrossRef] [PubMed] [Google Scholar]
  32. Kinder M, Greenplate AR, Grugan KD, et al., Engineered protease-resistant antibodies with selectable cell-killing functions. J Biol Chem. 2013;288:30843–54. [CrossRef] [PubMed] [Google Scholar]
  33. Brezski RJ, Luongo JL, Petrone D, et al., Human anti-IgG1 hinge autoantibodies reconstitute the effector functions of proteolytically inactivated IgGs. J Immunol. 2008;181:3183–92. [CrossRef] [PubMed] [Google Scholar]
  34. Falkenburg WJ, van Schaardenburg D, Ooijevaar-de Heer P, et al., Anti-hinge antibodies recognize IgG subclass- and protease-restricted neoepitopes. J Immunol. 2017;198:82–93. [CrossRef] [PubMed] [Google Scholar]
  35. Fan X, Brezski RJ, Deng H, et al., A novel therapeutic strategy to rescue the immune effector function of proteolytically inactivated cancer therapeutic antibodies. Mol Cancer Ther. 2015;14:681–91. [Google Scholar]
  36. Zhang N, Deng H, Fan X, et al., Dysfunctional antibodies in the tumor microenvironment associate with impaired anticancer immunity. Clin Cancer Res. 2015;21:5380–90. [CrossRef] [PubMed] [Google Scholar]
  37. Wang Y, Shi Q, Lv H, et al., IgG-degrading enzyme of Streptococcus pyogenes (IdeS) prevents disease progression and facilitates improvement in a rabbit model of Guillain-Barré syndrome. Exp Neurol. 2017;291:134–40. [CrossRef] [PubMed] [Google Scholar]
  38. Jordan SC, Lorant T, Choi J, et al., IgG Endopeptidase in highly sensitized patients undergoing transplantation. N Engl J Med. 2017;377:442–53. [Google Scholar]
  39. Lonze BE, Tatapudi VS, Weldon EP, et al., IdeS (Imlifidase): A novel agent that cleaves human IgG and permits successful kidney transplantation across high-strength donor-specific antibody. Ann Surg. 2018;268:488–96. [CrossRef] [PubMed] [Google Scholar]
  40. Kizlik-Masson C, Deveuve Q, Zhou Y, et al., Cleavage of anti-PF4/heparin IgG by a bacterial protease and potential benefit in heparin-induced thrombocytopenia. Blood. 2019;133:2427–35. [Google Scholar]

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