SyntIV uses synthetic immunology and virology to bioengineer innovative biomolecules, including molecular biosensors & tools, therapeutics, and vaccines. SyntIV is partially owned by the University of Minnesota and has a license to further develop new biomolecules discovered in the Herschhorn Lab at the University of Minnesota.

Leadership

Alon Herschhorn, Ph.D, Founder and Chief Executive of Operations

A tenured Associate Professor at the Department of Medicine, University of Minnesota Link

Selected publications

  • Parthasarathy, D., Pothula, K.R., Ratnapriya, S., Cervera-Benet, H, Parsons, R., Huang, X., Sammour, S., Janowska, K., Harris, M., Sodroski, J., Acharya, P. & Herschhorn, A. (2024). Conformational flexibility of HIV-1 Envelope glycoproteins modulates transmitted / founder sensitivity to broadly neutralizing antibodies. Nature Communications. 15(1):7334. PMID: 39187497. doi: 10.1038/s41467-024-51656-4. PDF

  • Mazurov, D. & Herschhorn A. (2024). Ultrasensitive quantification of HIV-1 cell-to-cell transmission in primary human CD4+ T cells measures viral sensitivity to broadly neutralizing antibodies. mBio 15(1), e0242823. PMID: 38063394. doi: 10.1128/mbio.02428-23. PDF

  • Ratnapriya, S., Harris, M., Chov, A., Herbert, Z., Vrbanac, V., Deruaz, M., Sodroski, J. & Herschhorn, A. (2021). Intra- and extra-cellular environments contribute to the fate of HIV-1 infection. Cell Reports 36(9), 109622. PMID: 34469717. doi: 10.1016/j.celrep.2021.109622. PDF

  • Herschhorn, A., Gu, C., Moraca, F., Ma, X., Farrell, M. Smith, A.B., Pancera, M., Kwong, P.D., Schön, A., Freire, E., Abrams C., Blanchard, S.C., Mothes, W. & Sodroski, J.G. (2017). The β20-β21 of gp120 is a regulatory switch for HIV-1 Env conformational transitions. Nature Communications 8(1), 1049. PMID: 29051495. doi: 10.1038/s41467-017-01119-w. PDF

  • Herschhorn, A., Ma, X., Gu, C., Castillo-Menendez, L., Melillo, B., Terry, D.S., Smith, AB, Blanchard, S.C., Munro, J.B., Mothes, W., Finzi, A., & Sodroski, J. (2016). Release of gp120 restrains leads to a functional intermediate state of the HIV-1 envelope glycoproteins. mBio 7, e01598-16. doi: 10.1128/mbio.01598. PDF    

  • Herschhorn, A., Gu, C., Espy, N., Richard, J., Finzi, A., & Sodroski, J. G. (2014). A broad HIV-1 inhibitor blocks envelope glycoprotein transitions critical for entry. Nature Chemical Biology 10(10), 845–852. PMID: 25174000. doi: 10.1038/nchembio.1623. Link