About

Joshua LaBaer is a leading investigator in personalized diagnostics, focusing on discovering and validating biomarkers for early detection of major illnesses such as cancer and diabetes. During the coronavirus pandemic, he repurposed resources to accelerate testing, establishing the ASU Biodesign Clinical Testing Laboratory, the first in the U.S. to offer public saliva tests for coronavirus, now accredited by the College of American Pathologists. His research lab is also one of four nationwide Capacity Building Centers in the NIH SeroNet tracking immune responses to COVID-19. Recruited to Arizona State University in 2009 as the first Piper Chair in Personalized Medicine, LaBaer has served as executive director of the Biodesign Institute since 2016 and directs the Biodesign Virginia G. Piper Center for Personalized Diagnostics. Previously, he founded and directed the Harvard Institute of Proteomics. LaBaer's research applies open reading frame clones to high-throughput protein function studies and he invented the Nucleic Acid Programmable Protein Array (NAPPA) technology, widely used in biomedical research. He has published over 250 original research works and was honored with the 2020 Jon W. McGarity Arizona Bioscience Leader of the Year Award. LaBaer earned his MD and PhD in biochemistry and biophysics from the University of California, San Francisco, followed by medical residency and oncology fellowship at Brigham and Women’s Hospital and Dana-Farber Cancer Institute, respectively. His research interests center on personalized medicine, emphasizing the development of novel therapeutics and diagnostic tests tailored to individual molecular disease variants. His lab employs multidisciplinary approaches including molecular biology, biochemistry, informatics, and robotics to understand protein functions and dysfunctions in disease. The FLEXGene Repository, developed under his leadership, provides a sequence-verified collection of full-length cDNAs for high-throughput protein function screening. LaBaer's NAPPA technology overcomes challenges of traditional protein microarrays by producing proteins in situ from plasmid DNA, enabling simultaneous functional testing of thousands of proteins. His lab uses NAPPA to identify autoantibody biomarkers for cancers and Type I diabetes, develop vaccines, and screen for antibodies against pathogens. Additionally, his group explores kinase activity and drug selectivity using NAPPA, and integrates NAPPA with surface plasmon resonance imaging for high-throughput, label-free detection of protein interactions. His cell-based research employs ectopic protein expression and RNA interference with viral vectors and robotics to study protein functions in vivo, particularly in breast cancer progression.

Research topics

• Biology
• Immunology
• Medicine
• Computational biology
• Internal medicine
• Genetics
• Cancer research
• Computer Science
• Gastroenterology
• Data science
• Bioinformatics
• Cell biology
• Chemistry
• Materials science
• Virology
• Engineering

Selected publications

• Abstract 2529: High throughput immunoproteomics for cancer biomarker discovery

  Cancer Research · 2026-04-03

  article1st authorCorresponding

  Abstract Background: Early detection of lung cancer (LC) remains a critical unmet need. While computed tomography (CT) screening saves lives by detecting cancer at early stages, its utility is limited by high false positive rates and insufficient sensitivity. These limitations lead to unnecessary surgeries and missed malignancies, particularly in individuals presenting with indeterminate pulmonary nodules (IPNs). Objective: Our overarching goal is to develop circulating biochemical biomarkers that improve the specificity of CT screening for LC by differentiating malignant from benign IPNs. Methods: We applied a high-throughput systems immunoproteomics strategy to discover serum biomarkers able to discriminate between malignant and benign IPNs. This integrated approach profiles three classes of circulating biomarkers: autoantibodies, anti-microbial antibodies, and serum proteins. Results: In the discovery phase, we profiled IgG and IgA autoantibodies using Nucleic Acid Programmable Protein Array (NAPPA) against 13,330 full-length human proteins, along with microbial antibodies against 8,820 microbial antigens. These analyses were conducted using serum from 144 lung cancer cases and 143 benign controls from Vanderbilt University Medical Center. Antibodies with significant enrichment in cases (odds ratio p < 0.05 in the top decile) were prioritized, yielding 112 autoantibodies and 70 microbial antibodies associated with malignancy, as well as 50 autoantibodies and 230 microbial antibodies associated with benign disease. In the validation phase, we assessed the prioritized antibody candidates in 319 subjects from the Detection of Early Lung Cancer Among Military Personnel (DECAMP-1) cohort using our Multiplexed In-Solution Protein Array (MISPA). In parallel, we quantified 19 well-reported cancer-associated serum proteins across the same samples. A multimodal panel comprising 7 autoantibodies, 4 microbial antibodies, and 4 serum proteins achieved an area under the curve (AUC) of 0.81 in the discovery cohort and 0.74 in independent validation cohorts, showing improved discrimination of malignant versus benign nodules compared to clinical models alone. Additionally, to demonstrate clinical scalability, we confirmed performance of top markers in 46 cases and 230 controls from the German Lung Cancer Screening Intervention Study (LUSI) using the Meso Scale Discovery (MSD) electrochemiluminescence platform. Conclusions: These results demonstrate a fully integrated immunoproteomics pipeline for the discovery, validation, and potential clinical translation of multiplex antibody and protein biomarkers for lung cancer detection. Citation Format: Joshua LaBaer, Jin Park, Ji Qiu, Lusheng Song, Karen S. Anderson, Jennifer Molloy, Gomati Nandedkar, Daniel Woodley, Deborah Adams, Candyce McDaniel, Andruw Fierro, Renée Turzanski Fortner, Toria Trendler, Mingyue Wang, Leonid Dzantiev, Anu Mathew, Martin Stengelin, Wohlstadter Jacob. High throughput immunoproteomics for cancer biomarker discovery [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2026; Part 1 (Regular Abstracts); 2026 Apr 17-22; San Diego, CA. Philadelphia (PA): AACR; Cancer Res 2026;86(7 Suppl):Abstract nr 2529.

  PublisherDOI

• Abstract 3181: Mutant p53-specific TAZ/TEAD pathway dependency as a therapeutic opportunity for triple-negative breast cancer

  Cancer Research · 2026-04-03

  articleSenior author

  Abstract Background: Missense mutations in the TP53 tumor suppressor gene lead to gain-of-function (GOF) properties that affect differently tumor growth, metastasis, and resistance to therapies, but targeting mutant p53 is still a major clinical challenge. Using MCF10A cells expressing 10 prevalent TP53 mutations, we performed integrated phenotypic and molecular analyses to identify targetable genes and pathways in Triple-Negative Breast Cancer (TNBC) harboring specific p53 mutations and discovered TAZ/TEAD dysregulation as the key determinants of cell invasion and drug resistance. Methods: Based on our previous findings, we measured activation status of TEAD in drug-sensitive and resistant mutant p53-expressing cells and evaluated the differential drug response against single or combination treatment of the TEAD inhibitor GNE-7883 and the standard-of-care, doxorubicin. The TEAD activity was verified with a luciferase reporter, and cell viability was measured with phosphatase assays. Results: The TEAD-luciferase reporter assay showed that p53 G245S and R273H mutants but not R175H or Y163C had elevated activity of the Hippo pathway effector, TEAD. Treatment of GNE-7883 robustly inhibited the hyper-activation of TEAD specifically in the G245S and R273H cells. In viability assays, these "TEAD-addicted" cells uniquely displayed sensitivity to high dose of GNE-7883 monotherapy (IC ∼2.5 µM). Moreover, they also showed hypersensitivity to doxorubicin (IC = 14 nM), compared to the cells with wild-type p53 (IC = 250 nM). We were able to develop a synergistic, low-dose combination regimen (3.5 nM doxorubicin + 0.625-1.25 µM GNE-7883) that was cytotoxic for the cells with G245S and R273H mutants yet had minimal to no activity in the wild-type cells. In contrast, R175H and Y163C mutants were resistant to TEAD inhibition, requiring higher doses of GNE-7883 to observe an anti-cancer activity, emphasizing the selectivity of this vulnerability. Conclusion: We have established a synthetic lethal interaction between TEAD inhibition for a defined chemo-sensitive subgroup of GOF p53 mutants, G245S and R273H, for which the Hippo/TEAD pathway states appear to be a key dependency. We propose a precision approach to therapeutic strategy of combining low, non-toxic dose doxorubicin with TEAD inhibition to increase efficacy while decreasing toxicity. Our ongoing work is to validate these findings in more physiologically relevant models. Citation Format: Lydia Sakala, Yining Zhang, Jin G. Park, Joshua LaBaer, . Mutant p53-specific TAZ/TEAD pathway dependency as a therapeutic opportunity for triple-negative breast cancer [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2026; Part 1 (Regular Abstracts); 2026 Apr 17-22; San Diego, CA. Philadelphia (PA): AACR; Cancer Res 2026;86(7 Suppl):Abstract nr 3181.

  PublisherDOI

• Anti-Epstein-Barr virus (EBV) antibodies in EBV-associated gastric carcinoma

  Infectious Agents and Cancer · 2026-04-02

  articleOpen access

  About 10% of gastric carcinomas (GC) harbor monoclonal Epstein-Barr virus (EBV). Anti-EBV antibody profiles distinguished patients with EBV-associated GC (EBVaGC) from those with EBV-negative GC (EBVnGC) in a previous study. Therefore, we examined these markers in a larger cohort with patient samples from Japan, a high gastric cancer-risk population. Multi-microbial Nucleic Acid Programmable Protein Array was used to test stored sera from 102 EBVaGC and 131 EBVnGC patients. Among 89 IgG antibodies against EBV-specific antigens, 32 (36%) showed at least 10% seroprevalence in either EBVaGC or EBVnGC patients. Seropositivity of ten anti-EBV antibodies (LF2, BDLF2, BXLF1, BRLF1, BKRF3, BHRF1, BORF2, BZLF1, BNRF1, and BALF2) were significantly higher in EBVaGC patients than those with EBVnGC, with a maximal odds ratio of 22 (95% confidence interval: 5.2, 195) for anti-LF2. The ten antibodies collectively had an area under the receiver operating curve of 0.747 (95% CI: 0.683, 0.811). Five of these markers (LF2, BRLF1, BXLF1, BORF2, and BALF2) were among the seven discriminatory antibodies identified in the previous study. These differences in serological reactions were seen for proteins in the lytic infection phase, but not for those in the latent infection phase, consistent with the previous results. The present study confirms the utility of anti-EBV serology for non-invasive detection of EBVaGC.

  PublisherDOI

• The omicron variant of SARS-CoV-2 drove broadly increased seroprevalence in a public university setting

  PLOS Global Public Health · 2025-01-03 · 4 citations

  articleOpen accessCorresponding

  Omicron is the comparatively most transmissible and contagious variant of severe acute respiratory syndrome-coronavirus-2 (SARS-CoV-2). We conducted a seroprevalence study from March 1-3, 2022, to investigate the seroprevalence of SARS-CoV-2 antibodies among individuals aged 18 years and older after the Omicron outbreak. The seroprevalence of anti-receptor binding domain (RBD) antibodies was found to be 96.3% (95% CI 95.2-97.2%) compared to 88.2% (95% CI 86.1-90%) in our previous serosurvey. For anti-nucleocapsid (NC) antibodies, the seroprevalence was 39.1% (95% CI 36.6-41.7%) compared to 19.7% (95% CI 17.5-22.2%) earlier. Individuals that experienced breakthrough infections exhibited the highest levels of anti-RBD antibodies. Additionally, saliva samples showed promise as a potential diagnostic biofluid for measuring antibody levels, as they exhibited a strong agreement with the data obtained from serum samples. The near doubling of anti-NC reactivity, a proxy for history of infection, reflects the contagiousness of the omicron variant, but may also have been influenced by a more relaxed approach to precautions in the spring of 2022. Serosurveys repeated at regular intervals monitor the trend of infections in the community, delineate the geographical spread of the infection, and may guide containment measures in communities, and prompt response to future outbreaks.

  PublisherOA PDFDOI

• Abstract 7087: Sample-sparing immunoassays for early detection of cancer

  Cancer Research · 2025-04-21

  article

  Abstract Research Use Only (RUO) sample-sparing MULTI-ARRAY immunoassays have been developed for several well-established cancer markers. The primary focus of this project is the development of assays to support research of suspicious lung nodules, but many of these selected markers are also relevant to other cancer types. These immunoassays include a serology panel, two biomarker panels, and a single-marker assay. The serology panel includes assays to detect autoantibodies to p53, CTAG-1, and CTAG-2. This panel requires 25 μL of 2, 500-fold diluted serum or plasma. A biomarker panel requiring 25 μL of 100-fold diluted serum or plasma detects the following biomarkers: CA15-3, SCFR/Kit, ErbB2, IGFBP-2, MIF, MMP-2, MMP-9 (total), REG4, S100A6, and TNF-RI. A second biomarker panel requiring 25 μLof 10-fold diluted serum or plasma detects the following biomarkers: CA125, Ca19-9, CEACAM-5 (CEA), EGFR, VEGFR-1/Flt-1, FLT3L, HE4, MMP-3 (total), and osteopontin. Finally, an assay for the core lung cancer biomarker cytokeratin-19 was developed. All assays had dynamic ranges that span 3-4 logs and are sufficiently sensitive to measure native levels in commercially sourced samples from apparently healthy individuals. The assays were preliminarily evaluated using more than 100 commercially sourced serum or plasma samples from apparently healthy individuals and more than 100 commercially sourced serum or plasma samples from patients with lung or other cancers. Many of the biomarkers had significantly different concentrations in several cancers compared to samples from apparently healthy individuals. These RUO assays may be useful in identifying biomarkers for a multi-marker panel to study early cancer. Citation Format: Mingyue Wang, Jermaine Brown, Daniel Lee, Salvia Misaghian, Taron Gorham, Leonid Dzantiev, Anu Mathew, Martin Stengelin, Ji Qiu, Karen Anderson, Joshua LaBaer, George Sigal, Jacob Wohlstadter. Sample-sparing immunoassays for early detection of cancer [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 7087.

  PublisherDOI

• Supplementary Table S4 from Comparative Microbiomics Analysis of Antimicrobial Antibody Response between Patients with Lung Cancer and Control Subjects with Benign Pulmonary Nodules

  2025-11-26

  articleOpen access

  Supplementary Table S4 from Comparative Microbiomics Analysis of Antimicrobial Antibody Response between Patients with Lung Cancer and Control Subjects with Benign Pulmonary Nodules

  PublisherOA PDFDOI

• Supplementary Figure S3 from Comparative Microbiomics Analysis of Antimicrobial Antibody Response between Patients with Lung Cancer and Control Subjects with Benign Pulmonary Nodules

  2025-11-26

  articleOpen access

  Supplementary Figure S3 from Comparative Microbiomics Analysis of Antimicrobial Antibody Response between Patients with Lung Cancer and Control Subjects with Benign Pulmonary Nodules

  PublisherDOI

• The Serological Sciences Network (SeroNet) for COVID-19: Depth and Breadth of Serology Assays and Plans for Assay Harmonization

  UNC Libraries · 2025-04-17

  articleOpen access

  In October 2020, the National Cancer Institute (NCI) Serological Sciences Network (SeroNet) was established to study the immune response to COVID-19, and "to develop, validate, improve, and implement serological testing and associated technologies" (https://www.cancer.gov/research/key-initiatives/covid-19/coronavirus-research-initiatives/serological-sciences-network). SeroNet is comprised of 25 participating research institutions partnering with the Frederick National Laboratory for Cancer Research (FNLCR) and the SeroNet Coordinating Center. Since its inception, SeroNet has supported collaborative development and sharing of COVID-19 serological assay procedures and has set forth plans for assay harmonization. To facilitate collaboration and procedure sharing, a detailed survey was sent to collate comprehensive assay details and performance metrics on COVID-19 serological assays within SeroNet. In addition, FNLCR established a protocol to calibrate SeroNet serological assays to reference standards, such as the U.S. severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) serology standard reference material and first WHO international standard (IS) for anti-SARS-CoV-2 immunoglobulin (20/136), to facilitate harmonization of assay reporting units and cross-comparison of study data. SeroNet institutions reported development of a total of 27 enzyme-linked immunosorbent assay (ELISA) methods, 13 multiplex assays, and 9 neutralization assays and use of 12 different commercial serological methods. FNLCR developed a standardized protocol for SeroNet institutions to calibrate these diverse serological assays to reference standards. In conclusion, SeroNet institutions have established a diverse array of COVID-19 serological assays to study the immune response to SARS-CoV-2 and vaccines. Calibration of SeroNet serological assays to harmonize results reporting will facilitate future pooled data analyses and study cross-comparisons. <strong>IMPORTANCE</strong> SeroNet institutions have developed or implemented 61 diverse COVID-19 serological assays and are collaboratively working to harmonize these assays using reference materials to establish standardized reporting units. This will facilitate clinical interpretation of serology results and cross-comparison of research data.

  PublisherDOI

• Highly Sensitive Spatial Proteomics with Multicolor Cleavable Fluorescent Tyramide

  Chemical & Biomedical Imaging · 2025-04-11 · 2 citations

  articleOpen access

  High-resolution single-cell spatial proteomics offers transformative insights into cellular diversity, architecture, interactions, and functions within complex biological systems. However, the existing multiplexed protein imaging platforms face challenges such as limited detection sensitivity, constrained target multiplexing capacity, or technically demanding. To address these issues, we report a highly sensitive spatial proteomics approach, using multicolor cleavable fluorescent tyramide and off-the-shelf antibodies. This method employs horseradish peroxidase (HRP) to enzymatically deposit distinct fluorophores to stain varied target proteins. Through reiterative cycles of target labeling, fluorescence imaging, and fluorophore cleavage, this approach allows numerous proteins profiled at the optical resolution in the same specimen. Utilizing this technique, we quantified 38 proteins within a human formalin-fixed paraffin-embedded (FFPE) tonsil tissue, which represents the highest target multiplexing capacity achieved to date using tyramide signal amplification (TSA) methods. Analysis of ∼500,000 individual cells in the same tissue revealed distinct cell clusters based on their protein expression profiles and spatial microenvironment. By mapping the cells back to their original tissue locations, we observed specific tissue subregions are composed of unique cell clusters. Furthermore, we also studied the cell-cell interactions and found the cells from the same cluster often showed strong association, while the cells in the varied clusters usually avoided contact.

  PublisherDOI

• Nucleic Acid Programmable Protein Arrays for Autoantibody Discovery: A Step-by-Step Guide

  Methods in molecular biology · 2025-10-14

  articleSenior author
  PublisherDOI

Recent grants

• NIH Grant R01HG002923

  NIH · $1.3M · 2005

• Novel approaches to study immune responses to post translational modifications for cancer detection

  NIH · $2.6M · 2016–2022

• NIH Grant R33CA099191

  NIH · $2.2M · 2007

• NIH Grant S10RR019310

  NIH · $804k · 2006

• NIH Grant K08CA064166

  NIH · $413k · 2001

Frequent coauthors

• Karen S. Anderson

  86 shared

• Ji Qiu

  Anhui Medical University

  77 shared

• Garrick Wallstrom

  58 shared

• Jin G. Park

  Arizona State University

  53 shared

• Daniel W. Cramer

  Harvard University

  42 shared

• Jessica Wong

  Creighton University

  41 shared

• Lusheng Song

  Arizona State University

  35 shared

• Manuel Fuentes

  Centro de Investigación Biomédica en Red de Cáncer

  34 shared

Education

• M.D.

  University of California School of Medicine

  1990

• Ph.D., Biochemistry and Biophysics

  University of California School of Medicine

  1989

Awards & honors

• 2020 Jon W. McGarity Arizona Bioscience Leader of the Year A…