OYAGEN is a biotechnology company focused on discovering, developing and commercializing novel pharmaceutical therapies. The Company seeks to exploit RNA editing and DNA editing enzymes with a specific focus on HIV/AIDS. OyaGen has expanded its original business model to broadly include the discovery of novel drug leads for a range of infectious diseases. Over the past decade, OyaGen has developed drug discovery methods that have enabled it to explore vulnerabilities in HIV, Ebola and Coronaviruses.
The Company has patented and has in development lead compounds as first-in-class therapeutics with curative potential for HIV. These experimental therapeutics protect the body’s host defense system consisting of DNA editing enzymes from being targeted for degradation by the HIV Vif protein. This therapeutic approach enables the editing enzymes to attack and neutralize the ability of HIV to infect cells. Editing enzymes (a.k.a. APOBECs) are endogenous cellular proteins that can mutate and destroy viral genomes by chemically altering the coding information in RNA or DNA molecules. OyaGen believes that there is a significant opportunity to “harness the editing process” to create therapies for a number of disease states. This initial focus on HIV is driven by a series of patented groundbreaking discoveries by OyaGen’s scientists, some of which have been recently published and are listed below.
In addition, OyaGen has designed and developed methods for identifying vulnerabilities within the Ebola virus and Coronavirus and used this knowhow in the identification of experimental therapeutics that inhibit the infectivity of these viruses.
OyaGen’s long term goal is to deliver new therapeutic solutions to the industry for the development of next generation therapeutics that address current and future healthcare needs.
Bennett, R.P., Salter, J.D., Smith, H.C. (2018) A New Class of Antiretroviral Enabling Innate Immunity by Protecting APOBEC3 from HIV Vif-Dependent Degradation. Trends in Molecular Medicine Published online March 30, 2018 PMID:29609878. Review
Polevoda, P., Mcdougall, W.M., Bennett, R.P., Salter, J.D., Smith, H.C. (2016) Structural and functional assessment of APOBEC3G macromolecular complexes. Methods 107:10-22.
Bennett, R.P., Stewart, R.A., Hogan, P., Ptak, R.G., Mankowski, M.K., Hartman, T.L., Buckheit, R.W., Jr., Snyder, B.A., Salter, J.D., Morales, G.A., Smith, H.C. (2016) An analog of camptothecin inactive against Topoisomerase I is broadly neutralizing of HIV-1 through inhibition of Vif-dependent APOBEC3G degradation. Antiviral Research 136:51-9
Salter, J.D., Bennett, R.P., Polevoda, B. And Smith, H.C. (2016) The APOBEC Protein Family United by Structure, Divergent in Function. Trends in Biochemical Sciences, Cell Press. 41:578-94.
Salter, J.D., Morales, G.A. Smith, H.C. (2014) Structural Insights for HIV-1 Therapeutic Strategies Targeting Vif. Trends Biochem Sci. 39:373-80.
Smith, H.C. (2011) APOBEC3G: A Double Agent in Host Defense. Trends Biochem Sci. 36:239-44.
Miller, H.-J. Presnyak, V. & Smith, H.C. (2007) The dimerization domain of HIV-1 viral infectivity factor Vif is required to block virion incorporation of APOBEC3G. Retrovirology 4:81.