Christopher Taron, Ph.D.

Senior Director of Protein Science and Innovation

Chris is both an experienced scientist and research director having spent most of his career working at New England Biolabs, a leading life sciences enzyme and reagent company.  He has performed research for over 33 years on many topics related to the discovery, recombinant production, analytical characterization, and biotechnological and pharmaceutical application of enzymes.  In that role, he has made significant contributions to basic science with over 70 publications.  Chris is also an experienced R&D director having served for 18 years as the Scientific Director of the Protein Expression & Modification research division at New England Biolabs.  In that capacity, he led a department of researchers on a broad range of both applied and basic research topics in protein science.  He has also served on the both the corporate and scientific boards of several biotech companies.  Chris is a big-picture strategic thinker who excels at designing and implementing R&D programs, collaborations, and partnerships.  He is also passionate about mentoring and development of early-career scientists.

Education

1990 – BSc Biochemistry, Colby College, Waterville, Maine
1999 – PhD Biochemistry, University of Illinois at Urbana-Champaign

Research Profile Links

LinkedIn Profile – Chris Taron, Ph.D.

Google Scholar

Research Interests

My research interests lie within the fields of protein biochemistry and glycobiology (the study of the structure, function, and biology of sugars).  In humans, it is estimated that upwards of 50% of proteins may possess appended sugars (“glycans”) that can affect their structure, localization, and biological function.  In addition, most pharmaceutical protein drugs (e.g., antibodies, growth factors, etc) are glycoproteins and their glycans are often critical to the drug’s tissue distribution, survival in the bloodstream, and pharmaceutical potency.  Despite their importance to both basic biology and pharmaceutical science, characterization of glycans lags that of other important cellular compounds like DNA, RNA, proteins, and lipids.  Because of the enormous structural complexity glycans, better tools and analytical workflows are needed to improve the characterization of glycoproteins.  Such improvements will both impact pharmaceutical drug characterization and possibly enable the use of glycans to diagnose human disease.

We are currently establishing high-throughput screening methods to discover novel enzymes from microbes that populate unique and underexplored marine ecosystems.  This methodology enables discovery of novel enzymes that both expand our understanding of how enzymes act on glycans and yield new activities that can be applied to analytical and pharmaceutical problems.  Finally, a comprehensive enzyme discovery platform will help GMGI to explore the breadth of unique enzymes and metabolites produced in marine environments, to better understand microbial biology.

Education

1990 – BSc Biochemistry, Colby College, Waterville, Maine
1999 – PhD Biochemistry, University of Illinois at Urbana-Champaign

Showing only Selected Publications

1

Selected Publications

*for full list, see Google Scholar

Fossa, S., Anton, B.P., Kneller, D.W., Petralia, L.M.C., Boisvert, M.L., Ganatra, M.B., Vainauskas, S., Chan, S., Hokke, C.H., Foster, J.M and Taron, C.H. (2023) A novel family of sugar-specific phosphodiesterases that removes zwitterionic modifications of N-acetylglucosamine. J. Biol. Chem. 299(12), 105437.

Helms, A., Escobar, E.E., Vainauskas, S., Taron, C.H., and Brodbelt, J.S. (2023) Ultraviolet photodissociation fragmentation permits comprehensive characterization of O-glycopeptides cleaved with O-glycoprotease IMPa. Anal. Chem. 95(24), 9280-9287.

Chen, M., Assis, D.M., Benet, M., McClung, C.M., Gordon, E., Ghose, S., Dupard, S.J., Willetts, M., Taron, C.H. and Samuelson, J.C. (2023) Comparative site-specific N-glycoproteome analysis reveals aberrant N-glycosylation and give insights into mannose-6-phosphate pathway in cancer.  Commun. Biol. 6(1), 48-64.

Vainauskas, S., Guntz, H., McLeod, E., McClung, C., Ruse, C.I., Shi, X. and Taron, C.H. (2022) A broad-specificity O-glycoprotease that enables improved analysis of glycoproteins and glycopeptides containing intact complex O-glycans. Anal. Chem. 94(2),1060-1069.

Zatopek, K.M., Fossa, S.L., Bilotti, K., Caffrey, P.J., Chuzel, L., Gehring, A.M., Lohman, G.J.S., Taron, C.H., Gardner, A.F. (2021) Capillary electrophoresis-based functional genomics screening to discover novel archaeal DNA modifying enzymes. Appl. Environ. Micro. 88(2):e0213721.

Chuzel, L., Fossa, S.L., Boisvert, M.L., Cajic, S., Hennig, R., Ganatra, M.B., Reichl, U., Rapp, E. and Taron, C.H. (2021) Combining functional metagenomics and glycoanalytics to identify enzymes that improve structural characterization of sulfated N-glycans.  Microb. Cell Fact.  20(1), 162.  Part of a special article collection: Microbial Glycobiotechnology.

Ganatra, M.B., Potapov, V., Vainauskas, S., Francis, A.Z., McClung, C.M., Ruse, C.I., Ong, J.L. and Taron, C.H. (2021) A bi-specific lectin from the mushroom Boletopsis grisea and its application in glycoanalytical workflows. Sci. Rep. 11(1), 160.

Bule, B., Chuzel, L., Blagova, E., Wu, L., Grey, M.A., Henrissat, B., Rapp, E., Bertozzi, C.R., Taron, C.H. and Davies, G. (2019) Inverting family GH156 sialidases define a new catalytic motif for glycosidase action. Nat. Commun. 10(1), 4816.

Zaramela, L.S., Martino, C., Alisson-Silva, F., Rees, S., Diaz, S.L., Chuzel, L., Ganatra, M.B, Taron, C.H., Secrest, P., Zuñiga, C., Huang, J., Siegel, D., Chang, G., Varki, A. and Zengler, K. (2019) Gut bacteria responding to dietary change encode sialidases that exhibit preference for red meat-associated carbohydrates. Nat. Microbiol. 4, 2082-2089.

Chuzel, L., Ganatra, M.B., Rapp, E., Henrissat, B. and Taron, C.H. (2018) Functional metagenomics identifies an exosialidase with an inverting catalytic mechanism that defines a new glycoside hydrolase family (GH156). J. Biol. Chem. 293(47), 18138-18150.

Vainauskas, S., Kirk, C., Petralia, L., Guthrie, E.P., McLeod, E., Bielik, A., Luebbers, A., Foster, J., Hokke, C.H., Rudd, P.M., Shi, X. and Taron, C.H.  (2018) A novel broad specificity fucosidase capable of core α(1,6) fucose release from N-glycans labeled with urea-linked fluorescent dyes.  Sci. Rep. 8(1), 9504-9512.

Chen, M., Shi, X., Duke, R.M., Ruse, C.I., Dai, N., Taron, C.H. and Samuelson, J.C. (2017) An engineered high affinity Fbs1 carbohydrate binding protein for selective and unbiased capture of N-glycans and N-glycopeptides. Nat. Commun. 8, 15487-15501.

Vainauskas, S., Duke, R.M., McFarland, J., McClung, C., Ruse, C. and Taron, C.H. (2016) Profiling of core fucosylated N-glycans using a novel bacterial lectin that specifically recognizes a1,6 fucosylated chitobiose. Sci. Rep. 6, 34195-34206.

Albrecht, S., Vainauskas, S., Stöckmann, H., McManus, C., Taron, C.H. and Rudd, P.M.  (2016) Comprehensive profiling of glycosphingolipid glycans using a novel broad specificity endoglycoceramidase in a high-throughput workflow.  Anal. Chem. 88(9), 4795-4802.

Lauber, M.A., Yu, Y., Brousmiche, D.W., Hua, A., Koza, S.M., Magnelli, P., Guthrie, E.P., Taron, C.H. and Fountain, K.J.  (2015) Rapid preparation of released N-glycans for HILIC analysis using a novel fluorescence and MS-active labeling reagent.  Anal. Chem.  87(10), 5401-9.