Dr Céline Jasmin Prange

All Publications

• T cell engagers control solid tumors through clonal replacement and IL2-driven effector differentiation of CD8 T cells. bioRxiv : the preprint server for biology Obenaus, M., Poupault, C. L., McGinnis, C. S., Prange, C., Jiang, H., Su, L. L., Chen, X., Miao, Z., Muldoon, J. J., Yao, W., Waghray, D., Sun, Q., Eyquem, J., Hernández-López, R. A., Satpathy, A. T., Sage, J., Garcia, K. C. 2026

  Abstract

  Bispecific T cell engagers (TCEs) often exhibit limited efficacy in solid tumors, in part due to immunosuppressive cues in the tumor microenvironment and low expression of targetable tumor antigens. Therapeutic strategies to improve TCE target sensitivity and enhance T cell effector functions therefore have significant translational potential. Here, we engineered TCEs that induce T cell activation in vitro against the low-abundance target antigens, TRP2/Kb and DLL3. Despite in vitro activity in these models, TCE monotherapy showed limited control of tumor growth in immunocompetent mice. Leveraging this in vivo model of TCE treatment failure, we discovered that co-treatment with TCE and a CD25-biased Interleukin-2 (IL2) rescues anti-tumor activity. Further, multimodal single-cell transcriptomic and immune repertoire analyses revealed that TCE-IL2 combination therapy controlled tumors by recruiting and activating new CD8+ T cells into the tumor microenvironment. These findings demonstrate that TCE-mediated anti-tumor responses function through a CD8+ T cell clonal replacement mechanism that can be augmented by cytokine therapy.

  View details for DOI 10.64898/2025.12.04.692214

  View details for PubMedID 41573936

  View details for PubMedCentralID PMC12822708

• Mitoribosomal small subunit maturation involves formation of initiation-like complexes PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA Lenarcic, T., Niemann, M., Ramrath, D. J. F., Calderaro, S., Fluegel, T., Saurer, M., Leibundgut, M., Boehringer, D., Prange, C., Horn, E. K., Schneider, A., Ban, N. 2022; 119 (3)

  Abstract

  Mitochondrial ribosomes (mitoribosomes) play a central role in synthesizing mitochondrial inner membrane proteins responsible for oxidative phosphorylation. Although mitoribosomes from different organisms exhibit considerable structural variations, recent insights into mitoribosome assembly suggest that mitoribosome maturation follows common principles and involves a number of conserved assembly factors. To investigate the steps involved in the assembly of the mitoribosomal small subunit (mt-SSU) we determined the cryoelectron microscopy structures of middle and late assembly intermediates of the Trypanosoma brucei mitochondrial small subunit (mt-SSU) at 3.6- and 3.7-Å resolution, respectively. We identified five additional assembly factors that together with the mitochondrial initiation factor 2 (mt-IF-2) specifically interact with functionally important regions of the rRNA, including the decoding center, thereby preventing premature mRNA or large subunit binding. Structural comparison of assembly intermediates with mature mt-SSU combined with RNAi experiments suggests a noncanonical role of mt-IF-2 and a stepwise assembly process, where modular exchange of ribosomal proteins and assembly factors together with mt-IF-2 ensure proper 9S rRNA folding and protein maturation during the final steps of assembly.

  View details for DOI 10.1073/pnas.2114710118

  View details for Web of Science ID 000748778000018

  View details for PubMedID 35042777

  View details for PubMedCentralID PMC8784144