About

Sue Lim is a social scientist with a strong interest in how artificial intelligence (AI), extended reality (XR), and other emerging technologies shape human judgment, decision-making, and behavior across contexts. Her current work focuses on three broad streams of research: examining interpersonal dynamics underlying human-AI interaction in XR, designing emerging technology-based interventions for specific groups or populations, and leveraging AI and XR as methodological tools to study human decision-making and behavior more broadly. Sue Lim combines many methodological approaches to answer her research questions, including physiological and behavioral measures, computational methods, qualitative interviews, and self-reports. She holds a B.S. in Economics with a concentration in Marketing from the Wharton School of the University of Pennsylvania and a Ph.D. in Communication from Michigan State University. Before joining Purdue University, she was a Postdoctoral Researcher at Michigan State University, affiliated with the CARISMA Lab in the department of Communication.

Research topics

• Biochemistry
• Immunology
• Biology
• Cancer research

Selected publications

• CD40 agonistic-monovalent streptavidin fusion antibody for targeted neoantigen peptide delivery and potent cancer vaccination

  bioRxiv (Cold Spring Harbor Laboratory) · 2025-08-01

  preprintOpen access

  Abstract Cancer vaccines targeting patient-derived neoantigens offer great promise for personalized cancer therapy but face challenges in achieving targeted delivery to antigen-presenting cells (APCs) to elicit robust and durable cancer-specific immune responses. We synthesized an anti-mouse CD40 agonistic-monovalent streptavidin fusion antibody (αCD40-mSAs), which enables targeted delivery of biotinylated neoantigen peptides to APCs in draining lymph nodes (dLNs). We confirmed mSA expression on the engineered antibody and its strong binding affinities to mouse CD40 and biotin. Advanced microscopy demonstrated that αCD40-mSAs enhances homing to dLNs and intracellular delivery of neoantigen peptides to critical APC subsets, such as cDC1. The potent agonistic effects of αCD40-mSAs on dendritic cell maturation, activation, and antigen presentation were verified through in vitro assays. Vaccination with αCD40-mSAs elicited robust cancer-specific CD8⁺ T cell responses, leading to significant tumor regression and prevention in a mouse tumor model. These results support αCD40-mSAs as an ‘all-in-one’ vaccine delivery platform with multifunctional immunopharmacological advantages and strong translational potential for personalized cancer vaccination. Teaser αCD40-mSAs is an engineered anti-CD40 agonistic antibody designed to enhance cancer vaccine delivery.

  PublisherOA PDFDOI

• Abstract 6085: Engineered anti-CD40 agonist antibody as a novel cancer neoantigen vaccine carrier

  Cancer Research · 2025-04-21

  article

  Abstract Somatic mutations in cancer cells lead to the expression of neoantigens that can be targeted by personalized vaccines utilizing patient’s own host immune system to fight against cancer. However, current personalized cancer vaccines have shown poor clinical outcomes due to the lack of effective delivery methods. To address the issues, our study aims to develop a novel vaccine platform that targets dendritic cells (DCs) and delivers neoantigen peptides more effectively by an anti-CD40 agonistic antibody expressing monovalent streptavidins (αCD40-mSAs). The agonistic anti-CD40 antibody will target and activate DCs, and the mSA compartment will allow the easy and fast loading of two biotinylated payloads (e.g. peptides and RNAs) on each vaccine carrier. CHO cell-based recombinant protein production method was used to biosynthesize αCD40 and αCD40-mSAs. Cloning vectors were reconstructed using mouse IgG2a, incorporating peptide sequences from the anti-mouse CD40 agonist antibody (clone FGK45) and monovalent streptavidin. For the biophysical properties of produced αCD40-mSAs, Surface Plasmon Resonance (SPR) for mouse CD40 and fluorescence polarization for biotin binding of mSAs have been used. Biotin- ovalbumin (OVA) peptide loaded αCD40-mSAs were subcutaneously injected into the footpad of the mice, and the collected lymph nodes were imaged with confocal microscopy and checked subtype of immune cells using flow cytometry. Antigen-specific T-cell responses were evaluated seven days post-injection by collecting lymph nodes and spleen. We successfully produced αCD40-mSAs, confirmed by increased molecular weight on the light chain expressing monovalent streptavidin. Binding assays demonstrated high-affinity interactions with mouse CD40 and effective biotin binding by the mSA moiety. In vivo targeting studies using fluorescently labeled OVA peptides revealed that αCD40-mSAs significantly enhanced peptide uptake in lymph nodes, particularly by cDC1 cells and macrophages. There was a notable increase in antigen-specific T cells, with an increase of OVA-specific CD8+ T cells and increased production of cytokines IL-2 and IFN-γ upon restimulation when OVA peptides were loaded onto αCD40-mSAs. In conclusion, αCD40-mSAs represent an effective delivery platform for personalized cancer vaccines by targeting DCs and improving neoantigen peptide uptake, offering a promising strategy to boost vaccine efficacy in cancer immunotherapy. Citation Format: Dahee Jung, Xiaoying Cai, Wonkyung Oh, Seung-Oe Lim, Steve Lee. Engineered anti-CD40 agonist antibody as a novel cancer neoantigen vaccine carrier [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2025; Part 1 (Regular Abstracts); 2025 Apr 25-30; Chicago, IL. Philadelphia (PA): AACR; Cancer Res 2025;85(8_Suppl_1):Abstract nr 6085.

  PublisherDOI

• Abstract 4857: The role of tumor microenvironment lactic acid in the cancer cell resistance to anti-PD-L1 and anti-PD-1 blockade therapy

  Cancer Research · 2025-04-21

  articleSenior author

  Abstract Immune checkpoint blockade therapy targeting the PD-1/PD-L1 axis has shown remarkable clinical impact in multiple cancer types. However, despite its recent success, such impact has been shown to be limited to tumors encompassing specific tumor microenvironment characteristics. Furthermore, a significant proportion of initial responders eventually develop resistance. Combining PD-1/PD-L1 blockade with chemotherapy, radiotherapy, or targeted therapy have been suggested to overcome resistance, yet have been shown to be insufficient in fully accounting for resistance. Unlike normal, differentiated cells, most cancer cells produce large amounts of lactic acid. This metabolic property is often referred to as “aerobic glycolysis, ” a well-known metabolic reprogramming of cancer cells to sustain cell proliferation and a hallmark of cancer. Such property as well as others of the altered metabolism of cancer cells and its byproducts affect the anti-tumor immune response. Notably, glycolytic metabolites, such as lactate, regulate T cell proliferation and function. However, the mechanism behind how such metabolic alterations impact the cancer cells’ resistance to PD-1/PD-L1 blockade therapy remains unclear. Thus, we sought to decipher the role of tumor-cell derived lactic acid in PD-1/PD-L1 therapy resistance and propose new immunotherapeutic strategies to improve the efficacy of PD-1/PD-L1 blockade therapies. Here, we found that tumor cell-derived lactic acid renders the immunosuppressive tumor microenvironment in the PD-1/PD-L1 blockade-resistant tumors by inhibiting the interaction between the PD-L1 protein and anti-PD-L1 antibody. Furthermore, we showed that the combination therapy of targeting PD-L1 with our PD-L1 antibody-drug conjugate (PD-L1-ADC) and reducing lactic acid with the MCT-1 inhibitor, AZD3965, can effectively treat the PD-1/PD-L1 blockade resistant tumors. Altogether, the findings in this study uncover a new mechanism of how lactic acid induces an immunosuppressive tumor microenvironment and suggest a potential combination treatment strategy to overcome the tumor resistance to PD-1/PD-L1 blockade therapy and improve clinical outcomes. Citation Format: Alyssa Kim, Wonkyung Oh, Deepika Dhawan, Deborah W. Knapp, Seung-Oe Lim. The role of tumor microenvironment lactic acid in the cancer cell resistance to anti-PD-L1 and anti-PD-1 blockade therapy [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2025; Part 1 (Regular Abstracts); 2025 Apr 25-30; Chicago, IL. Philadelphia (PA): AACR; Cancer Res 2025;85(8_Suppl_1):Abstract nr 4857.

  PublisherDOI

• Lactic acid inhibits the interaction between PD-L1 protein and PD-L1 antibody in the PD-1/PD-L1 blockade therapy-resistant tumor

  Molecular Therapy · 2024-12-31 · 16 citations

  articleSenior author
  PublisherDOI

• Development of an Anti-canine PD-L1 Antibody and Caninized PD-L1 Mouse Model as Translational Research Tools for the Study of Immunotherapy in Humans

  Cancer Research Communications · 2023-05-03 · 17 citations

  articleOpen accessSenior authorCorresponding

  Immune checkpoint blockade therapy, one of the most promising cancer immunotherapies, has shown remarkable clinical impact in multiple cancer types. Despite the recent success of immune checkpoint blockade therapy, however, the response rates in patients with cancer are limited (∼20%–40%). To improve the success of immune checkpoint blockade therapy, relevant preclinical animal models are essential for the development and testing of multiple combination approaches and strategies. Companion dogs naturally develop several types of cancer that in many respects resemble clinical cancer in human patients. Therefore, the canine studies of immuno-oncology drugs can generate knowledge that informs and prioritizes new immuno-oncology therapy in humans. The challenge has been, however, that immunotherapeutic antibodies targeting canine immune checkpoint molecules such as canine PD-L1 (cPD-L1) have not been commercially available. Here, we developed a new cPD-L1 antibody as an immuno-oncology drug and characterized its functional and biological properties in multiple assays. We also evaluated the therapeutic efficacy of cPD-L1 antibodies in our unique caninized PD-L1 mice. Together, these in vitro and in vivo data, which include an initial safety profile in laboratory dogs, support development of this cPD-L1 antibody as an immune checkpoint inhibitor for studies in dogs with naturally occurring cancer for translational research. Our new therapeutic antibody and caninized PD-L1 mouse model will be essential translational research tools in raising the success rate of immunotherapy in both dogs and humans. Significance: Our cPD-L1 antibody and unique caninized mouse model will be critical research tools to improve the efficacy of immune checkpoint blockade therapy in both dogs and humans. Furthermore, these tools will open new perspectives for immunotherapy applications in cancer as well as other autoimmune diseases that could benefit a diverse and broader patient population.

  PublisherOA PDFDOI

• FIGURE 5 from Development of an Anti-canine PD-L1 Antibody and Caninized PD-L1 Mouse Model as Translational Research Tools for the Study of Immunotherapy in Humans

  2023-05-15

  preprintOpen accessSenior author

  <p>Evaluation of the caninized cPD-L1 chimeric antibody. <b>A,</b> 12C antibody binding on the BT549<sup>cPD-L1</sup> cells. <b>B,</b> Flow cytometric analysis of the 12C chimeric antibody on the BT549<sup>cPD-L1</sup> cells. cIgG serves as a negative control. <b>C,</b> 12C chimeric antibody binding to cPD-L1 and cPD-L2. <b>D,</b> Binding affinity (K<sub>D</sub>) analysis of 12C chimeric antibody by Octet. <b>E,</b> EC<sub>50</sub> of 12C chimeric antibody, 12C10E4. EC<sub>50</sub> = 0.419 μg/mL. The bound cPD-1 protein was quantified by measuring green fluorescence at the IncuCyte S3. <b>F</b> and <b>G,</b> Canine IO Panel (NanoString) analyses were used to query changes in gene expression upon activation of cPBMCs from three healthy pet dogs. The RNA from the resting and activated PBMCs was used for NanoString work. The Canine IO panel was used to query the changes in approximately 700 genes. Groupwise analyses were conducted using “Rosalind.” There were 65 genes that were differentially expressed when comparing control PBMCs with activated PBMCs (<i>P</i> < 0.05, FC > 1.5) including 30 upregulated and 35 downregulated genes. In the heatmap, each column consists of data from one sample. IFNγ (<b>H</b>) and TNFα (<b>I</b>) concentrations were analyzed in the activated canine PBMCs. <b>J</b> and <b>K,</b> Flow cytometric analysis of cPD-L1 protein expression on the K9TCC or the nuclear-restricted RFP-expressing K9TCC (K9TCC<sup>nRFP</sup>) cells using the 12C chimeric antibody. The endogenous PD-L1 expression was stimulated by 50 ng/mL canine IFNγ for 12 hours. cIgG served as a negative control. <b>L,</b> The quantitative RT-PCR analysis of cPD-L1 (<i>CD274</i>) mRNA expression in the K9TCC or K9TCC<sup>nRFP</sup> cells. <b>M,</b> The 12C chimeric antibody enhances the tumor cell killing. Canine bladder cancer, K9TCC cells were cocultured with cPBMCs that were activated with CD3 antibody (100 ng/mL) and IL2 (10 ng/mL) at a ratio of 1 tumor cell: 15 cPBMCs. The live tumor cell count at 72 hours is shown in the bar graph. <b>N,</b> IFNγ concentrations were analyzed in the medium from the coculture of the K9TCC cells and activated cPBMCs with/without the 12C chimeric antibody treatment.</p>

  PublisherDOI

• FIGURE 2 from Development of an Anti-canine PD-L1 Antibody and Caninized PD-L1 Mouse Model as Translational Research Tools for the Study of Immunotherapy in Humans

  2023-05-15

  preprintOpen accessSenior author

  <p>The high-throughput screening of therapeutic antibodies. <b>A,</b> Schematic diagram of the cPD-L1 antibody binding assay. BT549 cells expressing cPD-L1 were seeded on 96-well or 384-well plates. cPD-L1 antibodies (from hybridomas) and Alexa Fluor 488–conjugated anti-mouse IgG Fc-specific secondary antibody were added, and then green fluorescence signal was measured to quantify the amount of bound PD-L1 antibody by IncuCyte S3. <b>B,</b> A representative result of the cPD-L1 antibody binding assay. Kinetic graphs from each well of a 96-well plate showing quantitative binding of cPD-L1 antibodies on BT549 cells expressing cPD-L1 at 6-hour time intervals. The positive clones are highlighted in red (A2, I6, and I11). <b>C,</b> Representative images (at 18 hours) of cPD-L1 antibody binding. Green fluorescent merged images of cPD-L1–expressing cells are shown. <b>D,</b> Schematic diagram of the cPD-L1/cPD-1 blockade assay. BT549 cells expressing cPD-L1 were seeded on 96-well or 384-well plates. cPD-1-human IgG Fc (hFc) protein, Alexa Fluor 488–conjugated anti-human IgG Fc-specific secondary antibody and/or cPD-L1 antibody were added, and then green fluorescence signal was measured to quantify the amount of bound PD-1 protein by IncuCyte S3. <b>E,</b> A representative result of the cPD-L1/cPD-1 blockade assay. Kinetic graphs from each well of a 96-well plate showing quantitative binding of cPD-1 protein on BT549 cells expressing cPD-L1 at 3-hour intervals after the addition of cPD-L1 antibodies. The positive clones that blocked the interaction of cPD-L1/cPD-1 proteins are highlighted in red (A4 and B8). <b>F,</b> Representative images (at 18 hours) of the cPD-L1/cPD-1 blockade. Green fluorescent merged images of cPD-L1–expressing cells are shown. Note the lack of fluorescence due to the antibody binding to PD-L1 and blocking the interaction with cPD-1.</p>

  PublisherDOI

• TABLE 1 from Development of an Anti-canine PD-L1 Antibody and Caninized PD-L1 Mouse Model as Translational Research Tools for the Study of Immunotherapy in Humans

  2023-05-15

  preprintOpen accessSenior author

  <p>Summary of potential adverse events with the initial cPD-L1 antibody administration to laboratory dogs</p>

  PublisherDOI

• Data from Development of an Anti-canine PD-L1 Antibody and Caninized PD-L1 Mouse Model as Translational Research Tools for the Study of Immunotherapy in Humans

  2023-05-15

  preprintOpen accessSenior author

  <div><p>Immune checkpoint blockade therapy, one of the most promising cancer immunotherapies, has shown remarkable clinical impact in multiple cancer types. Despite the recent success of immune checkpoint blockade therapy, however, the response rates in patients with cancer are limited (∼20%–40%). To improve the success of immune checkpoint blockade therapy, relevant preclinical animal models are essential for the development and testing of multiple combination approaches and strategies. Companion dogs naturally develop several types of cancer that in many respects resemble clinical cancer in human patients. Therefore, the canine studies of immuno-oncology drugs can generate knowledge that informs and prioritizes new immuno-oncology therapy in humans. The challenge has been, however, that immunotherapeutic antibodies targeting canine immune checkpoint molecules such as canine PD-L1 (cPD-L1) have not been commercially available. Here, we developed a new cPD-L1 antibody as an immuno-oncology drug and characterized its functional and biological properties in multiple assays. We also evaluated the therapeutic efficacy of cPD-L1 antibodies in our unique caninized PD-L1 mice. Together, these <i>in vitro</i> and <i>in vivo</i> data, which include an initial safety profile in laboratory dogs, support development of this cPD-L1 antibody as an immune checkpoint inhibitor for studies in dogs with naturally occurring cancer for translational research. Our new therapeutic antibody and caninized PD-L1 mouse model will be essential translational research tools in raising the success rate of immunotherapy in both dogs and humans.</p>Significance:<p>Our cPD-L1 antibody and unique caninized mouse model will be critical research tools to improve the efficacy of immune checkpoint blockade therapy in both dogs and humans. Furthermore, these tools will open new perspectives for immunotherapy applications in cancer as well as other autoimmune diseases that could benefit a diverse and broader patient population.</p></div>

  PublisherDOI

• FIGURE 2 from Development of an Anti-canine PD-L1 Antibody and Caninized PD-L1 Mouse Model as Translational Research Tools for the Study of Immunotherapy in Humans

  2023-05-15

  preprintOpen accessSenior author

  <p>The high-throughput screening of therapeutic antibodies. <b>A,</b> Schematic diagram of the cPD-L1 antibody binding assay. BT549 cells expressing cPD-L1 were seeded on 96-well or 384-well plates. cPD-L1 antibodies (from hybridomas) and Alexa Fluor 488–conjugated anti-mouse IgG Fc-specific secondary antibody were added, and then green fluorescence signal was measured to quantify the amount of bound PD-L1 antibody by IncuCyte S3. <b>B,</b> A representative result of the cPD-L1 antibody binding assay. Kinetic graphs from each well of a 96-well plate showing quantitative binding of cPD-L1 antibodies on BT549 cells expressing cPD-L1 at 6-hour time intervals. The positive clones are highlighted in red (A2, I6, and I11). <b>C,</b> Representative images (at 18 hours) of cPD-L1 antibody binding. Green fluorescent merged images of cPD-L1–expressing cells are shown. <b>D,</b> Schematic diagram of the cPD-L1/cPD-1 blockade assay. BT549 cells expressing cPD-L1 were seeded on 96-well or 384-well plates. cPD-1-human IgG Fc (hFc) protein, Alexa Fluor 488–conjugated anti-human IgG Fc-specific secondary antibody and/or cPD-L1 antibody were added, and then green fluorescence signal was measured to quantify the amount of bound PD-1 protein by IncuCyte S3. <b>E,</b> A representative result of the cPD-L1/cPD-1 blockade assay. Kinetic graphs from each well of a 96-well plate showing quantitative binding of cPD-1 protein on BT549 cells expressing cPD-L1 at 3-hour intervals after the addition of cPD-L1 antibodies. The positive clones that blocked the interaction of cPD-L1/cPD-1 proteins are highlighted in red (A4 and B8). <b>F,</b> Representative images (at 18 hours) of the cPD-L1/cPD-1 blockade. Green fluorescent merged images of cPD-L1–expressing cells are shown. Note the lack of fluorescence due to the antibody binding to PD-L1 and blocking the interaction with cPD-1.</p>

  PublisherDOI

Frequent coauthors

• Mien‐Chie Hung

  Asia University

  52 shared

• Chia-Wei Li

  Institute of Biomedical Sciences, Academia Sinica

  38 shared

• Weiya Xia

  The University of Texas MD Anderson Cancer Center

  34 shared

• Gabriel N. Hortobágyi

  31 shared

• Alyssa Min Jung Kim

  28 shared

• Shih-Shin Chang

  28 shared

• Wonkyung Oh

  25 shared

• Hirohito Yamaguchi

  25 shared

Education

• Ph.D., Biological Sciences

  Seoul National University

  2008

• M.S., Biological Sciences

  Seoul National University

  2003

• B.S., Biology Education

  Seoul National University

  2001