Gita Abhiraman is currently an MD-PhD candidate in the lab of Dr. Christopher Garcia, where she researches the structure and function of immune receptors. She is a PhD Candidate in the Immunology Program at Stanford. Gita received her bachelor's degree in physics with a focus in biophysics from Harvard University in 2018. She previously studied tumor-immune dynamics and helped to engineer sortase, a bacterial enzyme, for in vivo labeling under the mentorship of Dr. Stephanie Dougan at the Dana-Farber Cancer Institute.

Honors & Awards

  • Hertz Fellow, The Fannie and John Hertz Foundation (2021)

Education & Certifications

  • Bachelor of Arts, Harvard University (2018)

All Publications

  • Structure-based decoupling of the pro- and anti-inflammatory functions of interleukin-10. Science (New York, N.Y.) Saxton, R. A., Tsutsumi, N., Su, L. L., Abhiraman, G. C., Mohan, K., Henneberg, L. T., Aduri, N. G., Gati, C., Garcia, K. C. 2021; 371 (6535)


    Interleukin-10 (IL-10) is an immunoregulatory cytokine with both anti-inflammatory and immunostimulatory properties and is frequently dysregulated in disease. We used a structure-based approach to deconvolute IL-10 pleiotropy by determining the structure of the IL-10 receptor (IL-10R) complex by cryo-electron microscopy at a resolution of 3.5 angstroms. The hexameric structure shows how IL-10 and IL-10Ralpha form a composite surface to engage the shared signaling receptor IL-10Rbeta, enabling the design of partial agonists. IL-10 variants with a range of IL-10Rbeta binding strengths uncovered substantial differences in response thresholds across immune cell populations, providing a means of manipulating IL-10 cell type selectivity. Some variants displayed myeloid-biased activity by suppressing macrophage activation without stimulating inflammatory CD8+ T cells, thereby uncoupling the major opposing functions of IL-10. These results provide a mechanistic blueprint for tuning the pleiotropic actions of IL-10.

    View details for DOI 10.1126/science.abc8433

    View details for PubMedID 33737461

  • Generation of Ca2+-independent sortase A mutants with enhanced activity for protein and cell surface labeling PLOS ONE Jeong, H., Abhiraman, G. C., Story, C. M., Ingram, J. R., Dougan, S. K. 2017; 12 (12): e0189068


    Sortase A, a calcium-dependent transpeptidase derived from Staphylococcus aureus, is used in a broad range of applications, such as the conjugation of fluorescent dyes and other moieties to proteins or to the surface of eukaryotic cells. In vivo and cell-based applications of sortase have been somewhat limited by the large range of calcium concentrations, as well as by the often transient nature of protein-protein interactions in living systems. In order to use sortase A for cell labeling applications, we generated a new sortase A variant by combining multiple mutations to yield an enzyme that was both calcium-independent and highly active. This variant has enhanced activity for both N- and C-terminal labeling, as well as for cell surface modification under physiological conditions.

    View details for DOI 10.1371/journal.pone.0189068

    View details for Web of Science ID 000417033200027

    View details for PubMedID 29200433

    View details for PubMedCentralID PMC5714338