References
- Park J, Kwon M, Shin EC. Immune checkpoint inhibitors for cancer treatment. Arch Pharm Res. 2016;39:1577–12. doi:https://doi.org/10.1007/s12272-016-0850-5.
- Qureshi OS, Zheng Y, Nakamura K, Attridge K, Manzotti C, Schmidt EM, Baker J, Jeffery LE, Kaur S, Briggs Z, et al. Trans-endocytosis of CD80 and CD86: a molecular basis for the cell-extrinsic function of CTLA-4. Science. 2011;332:600–03. doi:https://doi.org/10.1126/science.1202947.
- Rowshanravan B, Halliday N, Sansom DM. CTLA-4: a moving target in immunotherapy. Blood. 2018;131:58–67. doi:https://doi.org/10.1182/blood-2017-06-741033.
- Tang F, Du X, Liu M, Zheng P, Liu Y. Anti-CTLA-4 antibodies in cancer immunotherapy: selective depletion of intratumoral regulatory T cells or checkpoint blockade? Cell Biosci. 2018;8:30. doi:https://doi.org/10.1186/s13578-018-0229-z.
- Simpson TR, Li F, Montalvo-Ortiz W, Sepulveda MA, Bergerhoff K, Arce F, Roddie C, Henry JY, Yagita H, Wolchok JD, et al. Fc-dependent depletion of tumor-infiltrating regulatory T cells co-defines the efficacy of anti-CTLA-4 therapy against melanoma. J Exp Med. 2013;210:1695–710. doi:https://doi.org/10.1084/jem.20130579.
- Ingram JR, Blomberg OS, Rashidian M, Ali L, Garforth S, Fedorov E, Fedorov AA, Bonanno JB, Le Gall C, Crowley S, et al. Anti-CTLA-4 therapy requires an Fc domain for efficacy. Proc Natl Acad Sci USA. 2018;115:3912–17. doi:https://doi.org/10.1073/pnas.1801524115.
- Arce Vargas F, Furness AJS, Litchfield K, Joshi K, Rosenthal R, Ghorani E, Solomon I, Lesko MH, Ruef N, Roddie C, et al. Fc effector function contributes to the activity of human anti-CTLA-4 antibodies. Cancer Cell. 2018;33:649–63 e4. doi:https://doi.org/10.1016/j.ccell.2018.02.010.
- Romano E, Kusio-Kobialka M, Foukas PG, Baumgaertner P, Meyer C, Ballabeni P, Michielin O, Weide B, Romero P, Speiser DE, et al. Ipilimumab-dependent cell-mediated cytotoxicity of regulatory T cells ex vivo by nonclassical monocytes in melanoma patients. Proc Natl Acad Sci USA. 2015;112:6140–45. doi:https://doi.org/10.1073/pnas.1417320112.
- Ipilimumab. Drugs R D. 2010;10:97–110. doi:https://doi.org/10.2165/11584510-000000000-00000. https://www.ncbi.nlm.nih.gov/pubmed/?term=Ipilimumab.+Drugs+R+D.+2010%3B10%3A97%E2%80%93110.
- Rotte A. Combination of CTLA-4 and PD-1 blockers for treatment of cancer. J Exp Clin Cancer Res. 2019;38:255. doi:https://doi.org/10.1186/s13046-019-1259-z.
- Tremelimumab. Drugs RD. 2010;10:123–32. doi:https://doi.org/10.2165/11584530-000000000-00000. https://www.ncbi.nlm.nih.gov/pubmed/?term=Tremelimumab.+Drugs+RD.+2010%3B10%3A123%E2%80%9332.
- Antonia S, Goldberg SB, Balmanoukian A, Chaft JE, Sanborn RE, Gupta A, Narwal R, Steele K, Gu Y, Karakunnel JJ, et al. Safety and antitumour activity of durvalumab plus tremelimumab in non-small cell lung cancer: a multicentre, phase 1b study. Lancet Oncol. 2016;17:299–308. doi:https://doi.org/10.1016/S1470-2045(15)00544-6.
- Bahig H, Aubin F, Stagg J, Gologan O, Ballivy O, Bissada E, Nguyen-Tan F-P, Soulières D, Guertin L, Filion E, et al. Phase I/II trial of durvalumab plus tremelimumab and stereotactic body radiotherapy for metastatic head and neck carcinoma. BMC Cancer. 2019;19:68. doi:https://doi.org/10.1186/s12885-019-5266-4.
- Fumet JD, Isambert N, Hervieu A, Zanetta S, Guion JF, Hennequin A, Rederstorff E, Bertaut A, Ghiringhelli F. Phase Ib/II trial evaluating the safety, tolerability and immunological activity of durvalumab (MEDI4736) (anti-PD-L1) plus tremelimumab (anti-CTLA-4) combined with FOLFOX in patients with metastatic colorectal cancer. ESMO Open. 2018;3:e000375. doi:https://doi.org/10.1136/esmoopen-2018-000375.
- Lee JY, Kim JW, Lim MC, Kim S, Kim HS, Choi CH, Yi JY, Park S-Y, Kim B-G. A phase II study of neoadjuvant chemotherapy plus durvalumab and tremelimumab in advanced-stage ovarian cancer: a Korean Gynecologic Oncology Group Study (KGOG 3046), TRU-D. J Gynecol Oncol. 2019;30:e112. doi:https://doi.org/10.3802/jgo.2019.30.e112.
- He M, Chai Y, Qi J, Zhang CWH, Tong Z, Shi Y, Yan J, Tan S, Gao GF. Remarkably similar CTLA-4 binding properties of therapeutic ipilimumab and tremelimumab antibodies. Oncotarget. 2017;8:67129–39. doi:https://doi.org/10.18632/oncotarget.18004.
- Selby MJ, Engelhardt JJ, Quigley M, Henning KA, Chen T, Srinivasan M, Korman AJ. Anti-CTLA-4 antibodies of IgG2a isotype enhance antitumor activity through reduction of intratumoral regulatory T cells. Cancer Immunol Res. 2013;1:32–42. doi:https://doi.org/10.1158/2326-6066.CIR-13-0013.
- Fiegle E, Doleschel D, Koletnik S, Rix A, Weiskirchen R, Borkham-Kamphorst E, Kiessling F, Lederle W. Dual CTLA-4 and PD-L1 blockade inhibits tumor growth and liver metastasis in a highly aggressive orthotopic mouse model of colon cancer. Neoplasia. 2019;21:932–44. doi:https://doi.org/10.1016/j.neo.2019.07.006.
- Zhu L, Guo Q, Guo H, Liu T, Zheng Y, Gu P, Chen X, Wang H, Hou S, Guo Y, et al. Versatile characterization of glycosylation modification in CTLA4-Ig fusion proteins by liquid chromatography-mass spectrometry. mAbs. 2014;6:1474–85. doi:https://doi.org/10.4161/mabs.36313.
- Bongers J, Devincentis J, Fu J, Huang P, Kirkley DH, Leister K, Liu P, Ludwig R, Rumney K, Tao L, et al. Characterization of glycosylation sites for a recombinant IgG1 monoclonal antibody and a CTLA4-Ig fusion protein by liquid chromatography-mass spectrometry peptide mapping. J Chromatogr A. 2011;1218:8140–49. doi:https://doi.org/10.1016/j.chroma.2011.08.089.
- Chikuma S. CTLA-4, an essential immune-checkpoint for T-cell activation. Curr Top Microbiol Immunol. 2017;410:99–126. doi:https://doi.org/10.1007/82_2017_61.
- Movahedin M, Brooks TM, Supekar NT, Gokanapudi N, Boons GJ, Brooks CL. Glycosylation of MUC1 influences the binding of a therapeutic antibody by altering the conformational equilibrium of the antigen. Glycobiology. 2017;27:677–87. doi:https://doi.org/10.1093/glycob/cww131.
- Peiris D, Spector AF, Lomax-Browne H, Azimi T, Ramesh B, Loizidou M, Welch H, Dwek MV. Cellular glycosylation affects Herceptin binding and sensitivity of breast cancer cells to doxorubicin and growth factors. Sci Rep. 2017;7:43006. doi:https://doi.org/10.1038/srep43006.
- Yu C, Sonnen AF, George R, Dessailly BH, Stagg LJ, Evans EJ, Orengo CA, Stuart DI, Ladbury JE, Ikemizu S, et al. Rigid-body ligand recognition drives cytotoxic T-lymphocyte antigen 4 (CTLA-4) receptor triggering. J Biol Chem. 2011;286:6685–96. doi:https://doi.org/10.1074/jbc.M110.182394.
- Stamper CC, Zhang Y, Tobin JF, Erbe DV, Ikemizu S, Davis SJ, Stahl ML, Seehra J, Somers WS, Mosyak L, et al. Crystal structure of the B7-1/CTLA-4 complex that inhibits human immune responses. Nature. 2001;410:608–11. doi:https://doi.org/10.1038/35069118.
- Ramagopal UA, Liu W, Garrett-Thomson SC, Bonanno JB, Yan Q, Srinivasan M, Wong SC, Bell A, Mankikar S, Rangan VS, et al. Structural basis for cancer immunotherapy by the first-in-class checkpoint inhibitor ipilimumab. Proc Natl Acad Sci USA. 2017;114:E4223–E32. doi:https://doi.org/10.1073/pnas.1617941114.
- Metzler WJ, Bajorath J, Fenderson W, Shaw SY, Constantine KL, Naemura J, Leytze G, Peach RJ, Lavoie TB, Mueller L, Linsey PS. Solution structure of human CTLA-4 and delineation of a CD80/CD86 binding site conserved in CD28. Nat Struct Biol. 1997;4:527–31. doi:https://doi.org/10.1038/nsb0797-527.
- Li D, Xu J, Wang Z, Gong Z, Liu J, Zheng Y, Li J, Li J. Epitope mapping reveals the binding mechanism of a functional antibody cross-reactive to both human and murine programmed death 1. mAbs. 2017;9:628–37. doi:https://doi.org/10.1080/19420862.2017.1296612.
- Fiser A, Sali A. Modeller: generation and refinement of homology-based protein structure models. Methods Enzymol. 2003;374:461–91.
- Pierce BG, Hourai Y, Weng Z. Accelerating protein docking in ZDOCK using an advanced 3D convolution library. PLoS One. 2011;6:e24657. doi:https://doi.org/10.1371/journal.pone.0024657.
- Danne R, Poojari C, Martinez-Seara H, Rissanen S, Lolicato F, Rog T, Vattulainen I. doGlycans-tools for preparing carbohydrate structures for atomistic simulations of glycoproteins, glycolipids, and carbohydrate polymers for GROMACS. J Chem Inf Model. 2017;57:2401–06. doi:https://doi.org/10.1021/acs.jcim.7b00237.
- Kutzner C, Pall S, Fechner M, Esztermann A, de Groot BL, Grubmuller H. More bang for your buck: improved use of GPU nodes for GROMACS 2018. J Comput Chem. 2019. doi:https://doi.org/10.1002/jcc.26011.
- Lee J, Cheng X, Swails JM, Yeom MS, Eastman PK, Lemkul JA, Wei S, Buckner J, Jeong JC, Qi Y, et al. CHARMM-GUI input generator for NAMD, GROMACS, AMBER, OpenMM, and CHARMM/OpenMM simulations using the CHARMM36 additive force field. J Chem Theory Comput. 2016;12:405–13. doi:https://doi.org/10.1021/acs.jctc.5b00935.
- Vangone A, Spinelli R, Scarano V, Cavallo L, Oliva R. COCOMAPS: a web application to analyze and visualize contacts at the interface of biomolecular complexes. Bioinformatics. 2011;27:2915–16. doi:https://doi.org/10.1093/bioinformatics/btr484.