Some of the content on this website requires JavaScript to be enabled in your web browser to function as intended. While the website is still usable without JavaScript, it should be enabled to enjoy the full interactive experience.

Skip to Main Navigation. Each navigation link will open a list of sub navigation links.

Skip to Main Content

Department of Molecular Biology|College of Agriculture and Natural Resources

Contact Don Jarvis

Department of Molecular Biology
University of Wyoming
1000 E. University Ave.
Laramie, WY 82071


Phone: (307) 766-4282

Jarvis Lab: Publications (last five years):

  1. Geisler, C. and Jarvis, D.L. 2009. Insect cell glycosylation patterns in the context of biopharmaceuticals, p. 165-191. In G. Walsh (ed.), Post-translational Modification of Protein Biopharmaceuticals. Wiley-Blackwell, Weinheim.
  2. Jarvis, D.L. 2009. Baculovirus–Insect Cell Expression Systems. Meth. Enzymol. 463:191-222.
  3. Geisler, C. and Jarvis, D.L. 2010. Identification of genes encoding N-glycan processing ß-N¬-acetylglucosaminidases from Trichoplusia ni and Bombyx mori: implications for N-glycosylation pathway engineering in baculovirus expression systems. Biotechnol. Progr. 26:34-44.
  4. Jarvis, D.L. 2010. Recombinant protein expression in baculovirus-infected insect cells. In Lorsch, J. ed., Methods Navigator Cookbook, Elsevier, Amsterdam.
  5. Hillar, A. and Jarvis, D.L. 2010. Re-visiting the endogenous capacity for recombinant glycoprotein sialylation by baculovirus-infected Tn-4h and DpN1 cells. Glycobiology 20:1323-1330.
  6. Geisler, C. and Jarvis, D.L. 2011. A clear understanding of Maackia amurensis lectin binding preferences is required for their effective utilization as tools for glycoanalysis. Glycobiology 21:988-993.
  7. Toth, A.M., Geisler, C. Aumiller, J.J., and Jarvis, D.L. 2011. Factors affecting recombinant Western equine encephalitis glycoprotein production in the baculovirus system. Protein Expr. Purif. 80:274-282.
  8. Aumiller, J.J., Mabashi-Asazuma, H., Hillar, A., Shi, X., and Jarvis, D.L. 2012. A new glycoengineered insect cell line with an inducibly-mammalianized protein N-glycosylation pathway. Glycobiology 22:417-428.
  9. Teulé, F., Miao, Y., Sohn, B.-H., Kim, Y.-S., Hull, J.J., Fraser, M.J., Lewis, R.V. and Jarvis, D.L. 2012. Silkworms transformed with chimeric silkworm/spider silk genes spin composite silk fibers with improved mechanical properties. Proc. Natl. Acad. Sci. U.S.A. 109:923-928.
  10. Geisler, C. and Jarvis, D.L. 2012. Substrate specificities and intracellular distributions of three N-glycan processing enzymes functioning at a key branch point in the insect N-glycosylation pathway. J. Biol. Chem. 287:7084-7097.
  11. Geisler, C., Kotu, V., Sharrow, M., Rendic, D., Poltl, G., Tiemeyer, M., Wilson, I.B.H., and Jarvis, D.L. 2012. The Drosophila neurally altered carbohydrate mutant has a defective Golgi GDP-fucose transporter. J. Biol. Chem. 287:29599-29609.
  12. Geisler, C. and Jarvis, D.L. 2012. Innovative use of a bacterial enzyme involved in sialic acid degradation to initiate sialic acid biosynthesis in glycoengineered insect cells. Metabol. Engr. 14:642-652.
  13. Mabashi-Asazuma, Shi, X., Geisler, C. and Jarvis, D.L. 2012. Impact of a human CMP-sialic acid transporter on recombinant glycoprotein sialylation in glycoengineered insect cells. Glycobiology, in press, 10/07/12.
  14. Phillips, A.T., Stauft, C.B., Aboellail, T.A., Toth, A.M., Jarvis, D.L., Powers, A.M., and Olson, K.E. 2013. Bioluminescent imaging and histopathologic characterization of WEEV neuroinvasion in outbred CD-1 mice. PLoS One 8:e53462.
  15. Lin, C.-H. and Jarvis, D.L. 2013. Utility of temporally distinct baculovirus promoters for constitutive and baculovirus-inducible transgene expression in transformed insect cells. J. Biotechnol. 165:11-17.
  16. Serena, M.S., Geisler, C., Metz, G.E., Corva, S.G., Mórtola, E.C., Jarvis, D.L., Echeverría, M.G. 2013. Expression and purification of Suid Herpesvirus-1 glycoprotein E in the baculovirus system and its use to diagnose Aujeszky’s disease in infected pigs. Prot. Expr. Purif., 90:1-8.
  17. Gao, Y., Aryal, R.P., Ju, T., Cummings, R.D., Gahlay, G., Jarvis, D.L., Matta, K.L., Vlahakis, J.Z., Szarek, W.A., and Brockhausen, I. 2013. Acceptor specificities and selective inhibition of recombinant human Gal- and GlcNAc-transferases that synthesize core structures 1, 2, 3 and 4 of O-glycans. Biochim. Biophys. Acta, 1830:4274-4281.
  18. Gerken, T.A., Revoredo, L., Thome, J., Tabak, L.A., Clausen, H., Vester-Christensen, M.B., 
Jarvis, D.L., Gahlay, G.K., and Moremen, K.W. 2013. The lectin domain of the polypeptide GalNAc transferase family of glycosyltransferases (ppGalNAc T’s) acts as a switch directing glycopeptide substrate glycosylation in an N- or C- direction further controlling mucin-type O-glycosylation. J. Biol Chem. 288:19900-19914.
  19. An, Y., Rininger, J.A., Jarvis, D.L., Jing, X., Ye, Z., Aumiller, J.J., Eichelberger, M., and Cipollo, J.F. 2013. Comparative glycomics analysis of influenza hemagglutinin (H5N1) produced in vaccine-relevant cell platforms. J. Proteome Res. 12:3707-3720.

(Last update 08/27/13)

Share This Page:

Footer Navigation

University of Wyoming Medallion
1000 E. University Ave. Laramie, WY 82071 // UW Operators (307) 766-1121 // Contact Us // Download Adobe Reader