John C Jewett

Photo of John C Jewett

John C Jewett

Associate Professor, Chemistry and Biochemistry-Sci
Member of the Graduate Faculty
Associate Professor, BIO5 Institute
Primary Department
Chemistry & Biochemistry
Department Affiliations
Chemistry & Biochemistry
BIO5 Institute
Contact
(520) 626-3627
jjewett@arizona.edu

Work Summary

We seek to develop tools and strategies to expedite the understanding and treatment of the dengue virus. These advances will be transferable to other areas of virology and biochemistry. Along these lines, we are engaged in three core synergistic projects to answer the following questions: (1) Do unnatural metabolites incorporated into DENV serve as reporters for host-pathogen interactions? (2) What are the host-pathogen interactions in DENV that are targetable for diagnosis or treatment? (3) Is there a chemical reaction between two small molecules that reports on the interaction between DENV and host proteins?

Research Interest

Our goal is to merge the fields of synthetic organic chemistry with virology. We develop new reactions (and re-appropriate old ones) to gain insight into how viruses infects new host cells. Additionally, we are working to develop new methods to probe protein-protein interactions through the use of small molecules.Viruses can rapidly evolve and new tools are required to meet this ever-changing threat. While vaccinations have tamed many historically deadly viral diseases, there are still rogue viruses for which no vaccination strategy is available. Dengue virus (DENV), the virus that is responsible for dengue fever, hemorrhagic fever, and shock syndrome, is one such pathogen. The WHO estimates that the mosquito-borne pathogen infects over 50 million people each year. With a rapid increase in severe, potentially fatal, disease forms, DENV poses a significant risk to the 2.5 billion people who live in DENV endemic regions.

Publications

Swarts, B. M., Holsclaw, C. M., Jewett, J. C., Alber, M., Fox, D. M., Siegrist, M. S., Leary, J. A., Kalscheuer, R., & Bertozzi, C. R. (2012). Probing the mycobacterial trehalome with bioorthogonal chemistry. Journal of the American Chemical Society, 134(39), 16123-16126.

PMID: 22978752;PMCID: PMC3466019;Abstract:

Mycobacteria, including the pathogen Mycobacterium tuberculosis, use the non-mammalian disaccharide trehalose as a precursor for essential cell-wall glycolipids and other metabolites. Here we describe a strategy for exploiting trehalose metabolic pathways to label glycolipids in mycobacteria with azide-modified trehalose (TreAz) analogues. Subsequent bioorthogonal ligation with alkyne-functionalized probes enabled detection and visualization of cell-surface glycolipids. Characterization of the metabolic fates of four TreAz analogues revealed unique labeling routes that can be harnessed for pathway-targeted investigation of the mycobacterial trehalome. © 2012 American Chemical Society.

He, J., Kimani, F. W., & Jewett, J. C. (2017). Rapid in Situ Generation of Benzene Diazonium Ions under Basic Aqueous Conditions from Bench-Stable Triazabutadienes. SYNLETT, 28(14), 1767-1770.

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