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. 2018 Sep;1(2):65-74.
doi: 10.1093/abt/tby009. Epub 2018 Oct 11.

Frontiers and Opportunities: Highlights of the 2nd Annual Conference of the Chinese Antibody Society

Affiliations
Free PMC article

Frontiers and Opportunities: Highlights of the 2nd Annual Conference of the Chinese Antibody Society

Hongyu Zhang et al. Antib Ther. 2018 Sep.
Free PMC article

Abstract

The Chinese Antibody Society (CAS) convened the second annual conference in Cambridge, MA, USA on 29 April 2018. More than 600 members from around the world attended the meeting. Invited speakers discussed the latest advancements in therapeutic antibodies with an emphasis on the progress made in China. The meeting covered a vast variety of topics including the current status of therapeutic antibodies, the progress of immuno-oncology, and biosimilars in China. The conference presentations also included the development of several novel antibodies such as antibodies related to weight loss, T-cell receptor-mimicking antibodies that target intracellular antigens, and tumor-targeting antibodies that utilize both innate and adaptive immune pathways. At the meeting, the CAS announced the launch of its official journal-Antibody Therapeutics-in collaboration with Oxford University Press. The conference was concluded by a panel discussion on how to bring a therapeutic drug developed in China to the USA for clinical trials.

Keywords: CAR T cells; Chinese Antibody Society; antibody therapeutics; biosimilars; bispecific antibodies.

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Figures

Figure 1
Figure 1
Binding affinity and ligand blocking measurements of Sintilimab and Nivolumab to PD-1 by SPR (Biacore) and cell-based assays. (A) Association and dissociation of Sintilimab to hPD-1 by SPR. (B) Association and dissociation of Nivolumab to hPD-1 by SPR. (C) Association and dissociation of Sintilimab to cynoPD-1 by SPR. (D) Association and dissociation of Nivolumab to cynoPD-1 by SPR. Antigens were serially diluted 2× from 25 nm (human) or 50 nM (cynomolgus) to 0.78 nm. (E) Affinity of Sintilimab to CHO-hPD-1 cells. (F) Affinity of Sintilimab to activated CD4+ T cells. (G–H) CHO-hPD1 cell-based ELISA with fixed concentrations of human PD-L1 (G) or PD-L2 (H). Figures show representative data from three independent experiments.
Figure 2
Figure 2
Functional activity of Sintilimab in cell-based bioassays. (A) Sintilimab tested in a luciferase-based ADCC functional assay. (B) Testing CDC activity of Sintilimab using a cell lysis assay. (C–D) MLR and effect of Sintilimab on T cell activation. moDC were generated and mixed with CD4+ T cells from a different donor for 5 days before detection of IL-2 (C) and IFN-γ (D) secretion by ELISA. (E–F) Luciferase reporter assay of IgG vs. Sintilimab, and Sintilimab vs. Nivolumab. Figures show representative data from three independent experiments.
Figure 3
Figure 3
In vivo hPD-1 knock-in mouse model to test anti-tumor efficacy of Sintilimab. (A) Tumor growth inhibition (TGI) of MC38 tumors in hPD-1 knock-in mice of individual animals treated with different doses of Sintilimab. (B) Effect of Sintilimab on percentage changes in mouse body weight (mean). (C) Changes in ratios of tumor infiltrating CD4+, CD8+ and Treg cells. For d8: IgG (n = 2); Sintilimab (n = 2). For d14, n = 3 for all groups.P values were calculated using a two-tailed t-test method.
Figure 4
Figure 4
Serum concentration-time profiles following a single intravenous infusion of 1, 6 and 30 mg/kg Sintilimab into cynomolgus monkeys. n = 6 animals/group (three males, three females). The Lower Limit of Quantification (LLOQ) of Sintilimab concentration ELISA assay was 500 ng/ml, and values below the LLOQ were interpreted as non-detectable during statistical analysis.

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