About

Timothy M. Harrison is an Associate Professor in the Department of English and the Committee on Conceptual and Historical Studies of Science at the University of Chicago. His work examines the conditions that enabled the literary representation of the first-person perspective in early modernity, with a focus on sixteenth- and seventeenth-century English literature. His research often relates literature to philosophy, theology, the sciences, and other cultural periods and regions. Harrison's scholarly interests include Renaissance poetry and poetics, British literature, critical theory, and objects of study. He has authored two books exploring the history of first-person experience in relation to human life, including 'Coming To: Consciousness and Natality in Early Modern England' (2020), which analyzes poetry's role in the emergence of consciousness through figures like Milton, Traherne, Descartes, and Locke, and 'John Donne's Physics' (2024), which reevaluates Donne’s representation of the body and embodiment. Harrison is engaged in ongoing projects that construct comparative literary histories of mindedness across early modern Eurasia and analyze Milton’s concept of human freedom through his work 'Paradise Lost.' His articles have received awards from the Milton Society of America and the John Donne Society, and his teaching has been recognized with awards for excellence in Ph.D. teaching and mentoring.

Research topics

• Immunology
• Genetics
• Medicine
• Biology
• Virology
• Computational biology

Selected publications

• Assessment of Immune Responses Against AAV Encoded Transgene Products

  The AAPS Journal · 2026-01-05 · 2 citations

  article
  PublisherDOI

• Evaluation of Cellular Immune Response to Adeno-Associated Virus-Based Gene Therapy

  The AAPS Journal · 2023 · 41 citations

  • Immunology
  • Biology
  • Computational biology
  PublisherOA PDFDOI

• Evaluation of the Humoral Response to Adeno-Associated Virus-Based Gene Therapy Modalities Using Total Antibody Assays

  The AAPS Journal · 2021 · 52 citations

  • Virology
  • Medicine
  • Immunology
  PublisherOA PDFDOI

• Interferons regulate the phenotype of wild-type and mutant herpes simplex viruses in vivo

  UNC Libraries · 2020-06-17

  articleOpen accessSenior author

  Mechanisms responsible for neuroattenuation of herpes simplex virus (HSV) have been defined previously by studies of mutant viruses in cultured cells. The hypothesis that null mutations in host genes can override the attenuated phenotype of null mutations in certain viral genes was tested. Mutants such as those in infected cell protein (ICP) 0, thymidine kinase, ribonucleotide reductase, virion host shutoff, and ICP34.5 are reduced in their capacity to replicate in nondividing cells in culture and in vivo. The replication of these viruses was examined in eyes and trigeminal ganglia for 1-7 d after corneal inoculation in mice with null mutations (-/-) in interferon receptors (IFNR) for type I IFNs (IFN-α/βR), type II IFN (IFN- γR), and both type I and type II IFNs (IFN-α/β/γR). Viral titers in eyes and ganglia of IFN-γR(-/-) mice were not significantly different from congenic controls. However, in IFN-α/βR(-/-) or IFN-α/β/γR(-/-) mice, growth of all mutants, including those with significantly impaired growth in cell culture, was enhanced by up to 1,000-fold in eyes and trigeminal ganglia. Blepharitis and clinical signs of infection were evident in IFN- α/βR(-/-) and IFN-α/β/γR(-/-) but not control mice for all viruses. Also, IFNs were shown to significantly reduce productive infection of, and spread from intact, but not scarified, corneas. Particularly striking was restoration of near-normal trigeminal ganglion replication and neurovirulence of an ICP34.5 mutant in IFN-α/βR(-/-) mice. These data show that IFNs play a major role in limiting mutant and wild-type HSV replication in the cornea and in the nervous system. In addition, the in vivo target of ICP34.5 may be host IFN responses. These experiments demonstrate an unsuspected role for host factors in defining the phenotypes of some HSV mutants in vivo. The phenotypes of mutant viruses therefore cannot be interpreted based solely upon studies in cell culture but must be considered carefully in the context of host factors that may define the in vivo phenotype.

  PublisherDOI

• Structure of a Plasmodium PIR protein ectodomain

  2020-08-03

  paratext1st authorCorresponding
  PublisherDOI

• RIFIN variable region bound to LILRB1 ectodomain

  2020-06-15

  paratext1st authorCorresponding
  PublisherDOI

• Abstract 543: Dinutuximab binds specifically to disialoganglioside-2

  Cancer Research · 2019-07-01 · 3 citations

  article

  Abstract Dinutuximab is a human/murine chimeric monoclonal antibody, approved for maintenance treatment of pediatric patients with high-risk neuroblastoma (NB) in the US, and currently under investigation in a phase III trial (NCT03098030) for 2nd line treatment of relapsed/refractory small cell lung cancer (SCLC). Despite four decades of development, the specificity of dinutuximab binding to its intended target, disialoganglioside-2 (GD2), has not been fully elucidated. Although GD2 is a relatively cancer cell specific antigen, other cell surface gangliosides are ubiquitously expressed on the outer membrane of healthy human cells. Therefore, the main goal of this study was to confirm binding specificity of dinutuximab to GD2. We also compared relative affinity of dinutuximab to GD2 with 14G2a, which is the original murine anti-GD2 antibody from which dinutuximab was derived. To measure dinutuximab and 14G2a binding kinetics to various relevant gangliosides (GD1a, GD1b, GM3, GD3, GM4, GM2 and GD2), an in vitro assay was developed and optimized using the Biacore surface plasmon resonance platform. The results showed that GD2 was the only ganglioside that binds to dinutuximab (relative KD=0.000337M). The relative affinity of GD2 to dinutuximab and 14G2a antibody were comparable and within 2-fold of each other (Table). In conclusion, dinutuximab specifically binds to GD2. The absence of binding to GM3, GD3, GD1a, or GD1b suggests that an exposed N-acetylgalactosamine (GalNAc) moiety is necessary for antibody recognition. The absence of binding to GM2 or GT2 (sugar moiety), which differ from GD2 by the number of sialic residues attached to the basal galactose moiety, suggests that the number of sialic acid residues is also critical for antibody recognition. GD2 binding kinetics of Dinutuximab and 14G2aLigandKD (M)ka (1/Ms)kd (1/s)Chi2 (RU2)Dinutuximab3.37E-042.48E+028.34E-020.78614G2a2.00E-047.11E+021.42E-010.0273 Citation Format: Shahriar Yaghoubi, Travis Harrison, Gerald Messerschmidt, Suzana Corritori. Dinutuximab binds specifically to disialoganglioside-2 [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2019; 2019 Mar 29-Apr 3; Atlanta, GA. Philadelphia (PA): AACR; Cancer Res 2019;79(13 Suppl):Abstract nr 543.

  PublisherDOI

• Abstract 543: Dinutuximab binds specifically to disialoganglioside-2

  Clinical Research (Excluding Clinical Trials) · 2019-07-01 · 1 citations

  article

  Dinutuximab is a human/murine chimeric monoclonal antibody, approved for maintenance treatment of pediatric patients with high-risk neuroblastoma (NB) in the US, and currently under investigation in a phase III trial (NCT03098030) for 2nd line treatment of relapsed/refractory small cell lung cancer (SCLC). Despite four decades of development, the specificity of dinutuximab binding to its intended target, disialoganglioside-2 (GD2), has not been fully elucidated. Although GD2 is a relatively cancer cell specific antigen, other cell surface gangliosides are ubiquitously expressed on the outer membrane of healthy human cells. Therefore, the main goal of this study was to confirm binding specificity of dinutuximab to GD2. We also compared relative affinity of dinutuximab to GD2 with 14G2a, which is the original murine anti-GD2 antibody from which dinutuximab was derived. To measure dinutuximab and 14G2a binding kinetics to various relevant gangliosides (GD1a, GD1b, GM3, GD3, GM4, GM2 and GD2), an in vitro assay was developed and optimized using the Biacore surface plasmon resonance platform. The results showed that GD2 was the only ganglioside that binds to dinutuximab (relative KD=0.000337M). The relative affinity of GD2 to dinutuximab and 14G2a antibody were comparable and within 2-fold of each other (Table). In conclusion, dinutuximab specifically binds to GD2. The absence of binding to GM3, GD3, GD1a, or GD1b suggests that an exposed N-acetylgalactosamine (GalNAc) moiety is necessary for antibody recognition. The absence of binding to GM2 or GT2 (sugar moiety), which differ from GD2 by the number of sialic residues attached to the basal galactose moiety, suggests that the number of sialic acid residues is also critical for antibody recognition.GD2 binding kinetics of Dinutuximab and 14G2aLigandKD (M)ka (1/Ms)kd (1/s)Chi2 (RU2)Dinutuximab3.37E-042.48E+028.34E-020.78614G2a2.00E-047.11E+021.42E-010.0273Citation Format: Shahriar Yaghoubi, Travis Harrison, Gerald Messerschmidt, Suzana Corritori. Dinutuximab binds specifically to disialoganglioside-2 [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2019; 2019 Mar 29-Apr 3; Atlanta, GA. Philadelphia (PA): AACR; Cancer Res 2019;79(13 Suppl):Abstract nr 543.

  PublisherDOI

• GCC Consolidated Feedback to ICH on the 2019 ICH M10 Bioanalytical Method Validation Draft Guideline

  Bioanalysis · 2019-09-01 · 29 citations

  articleOpen access

  , 2019. This GCC meeting was organized to discuss the contents of the 2019 ICH M10 Bioanalytical Method Validation Draft Guideline published in February 2019 and consolidate the feedback of the GCC members. In attendance were 63 senior-level participants from eight countries representing 44 bioanalytical CRO companies/sites. This event represented a unique opportunity for CRO bioanalytical experts to share their opinions and concerns regarding the ICH M10 Bioanalytical Method Validation Draft Guideline and to build unified comments to be provided to the ICH.

  PublisherOA PDFDOI

• The MG-RAST API explorer: an on-ramp for RESTful query composition

  BMC Bioinformatics · 2019-11-08 · 14 citations

  articleOpen access

  BACKGROUND: The MG-RAST API provides search capabilities and delivers organism and function data as well as raw or annotated sequence data via the web interface and its RESTful API. For casual users, however, RESTful APIs are hard to learn and work with. RESULTS: We created the graphical MG-RAST API explorer to help researchers more easily build and export API queries; understand the data abstractions and indices available in MG-RAST; and use the results presented in-browser for exploration, development, and debugging. CONCLUSIONS: The API explorer lowers the barrier to entry for occasional or first-time MG-RAST API users.

  PublisherOA PDFDOI

Frequent coauthors

• Kasturi Haldar

  University of Notre Dame

  76 shared

• Narla Mohandas

  70 shared

• Benjamin U. Samuel

  64 shared

• Marion E. Reid

  54 shared

• Sean C. Murphy

  University of Washington

  53 shared

• Kaye D. Speicher

  The Wistar Institute

  49 shared

• Philip S. Low

  Purdue University West Lafayette

  49 shared

• David W. Speicher

  49 shared

Awards & honors

• James Holly Hanford Award from the Milton Society of America
• Albert C. Labriola Award from the Milton Society of America
• John Donne Society’s Distinguished Publication Award
• Milton Society of America’s James Holly Hanford Award for be…
• Milton Society of America’s Albert C. Labriola Award