Bio

Aadit is an MD candidate at Stanford with a BS in Biomedical Engineering from Washington University and an MPhil in Bioscience Enterprise from the University of Cambridge. While completing these degrees, he conducted 4 years of immunology/infectious diseases research as well as led the development of a medical device through to acquisition. While at Cambridge and Stanford, he gained exposure to operating and investing experience in therapeutics (particularly immuno-oncology and genetic medicines) with prior work spanning Flagship Pioneering, Tessera Therapeutics, and 5AM Ventures. As an advocate for the larger student innovation community, Aadit oversaw the national network of biomedical incubators: Sling Health. As National Network President, he supported more than 1000 students across 15 institutions and reported outcomes twice in Nature Biotechnology.

Education & Certifications

  • Bachelor of Science, Washington University, UG Bioengineering (2019)
  • Master of Philosophy, University of Cambridge (2021)
  • MPhil, University of Cambridge, Bioscience Enterprise
  • BS, Washington University in St. Louis, Biomedical Engineering

Patents

  • Aadit Shah. "United States Patent WO2018201008A1 Non-mydriatic mobile retinal imager", Spect Inc

Contact

  • Academic
    aadits@stanford.edu
    University - Student Department: School of Medicine Position: Graduate, Medicine

Additional Info

Links

All Publications

  • Engineering Inducible Signaling Receptors to Increase Erythropoietic Output from Genome-Edited Hematopoietic Stem Cells Shah, A. P., Majeti, K., Luna, S., Porteus, M. H., Cromer, K. CELL PRESS. 2023: 419-420

    View details for Web of Science ID 001045144202047

  • Characterization of remote second-opinion oncology patients and associated changes in management. Shah, A. P., Shi, S., Shah, S. LIPPINCOTT WILLIAMS & WILKINS. 2022: E18563

    View details for Web of Science ID 000863680303717

  • A virtual innovation bootcamp to remotely connect and empower students to solve COVID-19-related medical problems. Nature biotechnology Russo, M. V., Appukutty, A. J., Shah, A. P., Mohan, H. K., Daniel, A. G., Pack, A., Xie, R. 2022; 40 (6): 976-979

    View details for DOI 10.1038/s41587-022-01352-9

    View details for PubMedID 35705707

  • Pan-protective anti-alphavirus human antibodies target a conserved E1 protein epitope CELL Kim, A. S., Kafai, N. M., Winkler, E. S., Gilliland, T., Cottle, E. L., Earnest, J. T., Jethva, P. N., Kaplonek, P., Shah, A. P., Fong, R. H., Davidson, E., Malonis, R. J., Quiroz, J. A., Williamson, L. E., Vang, L., Mack, M., Crowe, J., Doranz, B. J., Lai, J. R., Alter, G., Gross, M. L., Klimstra, W. B., Fremont, D. H., Diamond, M. S. 2021; 184 (17): 4414-+

    Abstract

    Alphaviruses are emerging, mosquito-transmitted pathogens that cause musculoskeletal and neurological disease in humans. Although neutralizing antibodies that inhibit individual alphaviruses have been described, broadly reactive antibodies that protect against both arthritogenic and encephalitic alphaviruses have not been reported. Here, we identify DC2.112 and DC2.315, two pan-protective yet poorly neutralizing human monoclonal antibodies (mAbs) that avidly bind to viral antigen on the surface of cells infected with arthritogenic and encephalitic alphaviruses. These mAbs engage a conserved epitope in domain II of the E1 protein proximal to and within the fusion peptide. Treatment with DC2.112 or DC2.315 protects mice against infection by both arthritogenic (chikungunya and Mayaro) and encephalitic (Venezuelan, Eastern, and Western equine encephalitis) alphaviruses through multiple mechanisms, including inhibition of viral egress and monocyte-dependent Fc effector functions. These findings define a conserved epitope recognized by weakly neutralizing yet protective antibodies that could be targeted for pan-alphavirus immunotherapy and vaccine design.

    View details for DOI 10.1016/j.cell.2021.07.006

    View details for Web of Science ID 000686554600007

    View details for PubMedID 34416146

    View details for PubMedCentralID PMC8382027

  • LDLRAD3 is a receptor for Venezuelan equine encephalitis virus NATURE Ma, H., Kim, A. S., Kafai, N. M., Earnest, J. T., Shah, A. P., Case, J., Basore, K., Gilliland, T. C., Sun, C., Nelson, C. A., Thackray, L. B., Klimstra, W. B., Fremont, D. H., Diamond, M. S. 2020; 588 (7837): 308-+

    Abstract

    Venezuelan equine encephalitis virus (VEEV) is a neurotropic alphavirus transmitted by mosquitoes that causes encephalitis and death in humans1. VEEV is a biodefence concern because of its potential for aerosol spread and the current lack of sufficient countermeasures. The host factors that are required for VEEV entry and infection remain poorly characterized. Here, using a genome-wide CRISPR-Cas9-based screen, we identify low-density lipoprotein receptor class A domain-containing 3 (LDLRAD3)-a highly conserved yet poorly characterized member of the scavenger receptor superfamily-as a receptor for VEEV. Gene editing of mouse Ldlrad3 or human LDLRAD3 results in markedly reduced viral infection of neuronal cells, which is restored upon complementation with LDLRAD3. LDLRAD3 binds directly to VEEV particles and enhances virus attachment and internalization into host cells. Genetic studies indicate that domain 1 of LDLRAD3 (LDLRAD3(D1)) is necessary and sufficient to support infection by VEEV, and both anti-LDLRAD3 antibodies and an LDLRAD3(D1)-Fc fusion protein block VEEV infection in cell culture. The pathogenesis of VEEV infection is abrogated in mice with deletions in Ldlrad3, and administration of LDLRAD3(D1)-Fc abolishes disease caused by several subtypes of VEEV, including highly virulent strains. The development of a decoy-receptor fusion protein suggests a strategy for the prevention of severe VEEV infection and associated disease in humans.

    View details for DOI 10.1038/s41586-020-2915-3

    View details for Web of Science ID 000591047800006

    View details for PubMedID 33208938

    View details for PubMedCentralID PMC7769003

  • Advancing healthcare technology education and innovation in academia NATURE BIOTECHNOLOGY Linderman, S. W., Appukutty, A. J., Russo, M. V., Shah, A. P., Javaherian, K. 2020; 38 (10): 1213-1217

    View details for DOI 10.1038/s41587-020-0689-7

    View details for Web of Science ID 000575176200027

    View details for PubMedID 33020629

https://orcid.org/0000-0001-8672-6643