Site-selective glycosylation of proteins: creating synthetic glycoproteins (original) (raw)

• Wold, F. In vivo chemical modification of proteins (post-translational modification). Ann. Rev. Biochem. 50, 783–814 (1981).
  Article CAS Google Scholar
• Walsh, C.T., Garneau-Tsodikova, S. & Gatto, G.J. Jr. Protein posttranslational modifications: the chemistry of proteome diversifications. Angew. Chem. Int. Ed. 44, 7342–7372 (2005).
  Article CAS Google Scholar
• Walsh, C.T. Posttranslational Modification of Proteins: Expanding Nature's Inventory (Roberts and Co. Press, Englewood, Colorado, 2005).
  Google Scholar
• Rademacher, T.W., Parekh, R.B. & Dwek, R.A. Glycobiology. Annu. Rev. Biochem. 57, 785–838 (1988).
  Article CAS Google Scholar
• Dwek, R.A. Glycobiology: toward understanding the function of sugars. Chem. Rev. 6, 683–720 (1996).
  Article Google Scholar
• Rudd, P.M. et al. Glycoforms modify the dynamic stability and functional activity of an enzyme. Biochemistry 33, 17–22 (1994).
  Article CAS Google Scholar
• Hamilton, S.R. et al. Humanization of yeast to produce complex terminally sialylated glycoproteins. Science 313, 1441–1443 (2006).
  Article CAS Google Scholar
• Li, H. et al. Optimization of humanized IgGs in glycoengineered Pichia pastoris. Nat. Biotechnol. 24, 210–215 (2006).
  Article CAS Google Scholar
• Bobrowicz, P. et al. Engineering of an artificial glycosylation pathway blocked in core oligosaccharide assembly in the yeast Pichia pastoris: Production of complex humanized glycoproteins with terminal galactose. Glycobiology 14, 757–766 (2004).
  Article CAS Google Scholar
• Hamilton, S.R. et al. Production of complex human glycoproteins in yeast. Science 301, 1244–1246 (2003).
  Article CAS Google Scholar
• Xie, J. & Schultz, P.G. A chemical toolkit for proteins—an expanded genetic code. Nat. Rev. Mol. Cell Biol. 7, 775–782 (2006).
  Article CAS Google Scholar
• Zhang, Z. et al. A new strategy for the synthesis of glycoproteins. Science 303, 371–373 (2004).
  Article CAS Google Scholar
• Xu, R. et al. Site-specific incorporation of the mucin-type N-acetylgalactosamine-β-O-threonine into protein in Escherichia coli. J. Am. Chem. Soc. 126, 15654–15655 (2004).
  Article CAS Google Scholar
• van Kasteren, S.I., Garnier, P.G. & Davis, B.G. Chemical methods for mimicking post-translational modifications. in Protein Engineering (Springer Verlag, Berlin and Heidelberg, 2007).
  Google Scholar
• Davis, B.G. Synthesis of glycoproteins. Chem. Rev. 102, 579–601 (2002).
  Article CAS Google Scholar
• Liu, L., Bennett, C.S. & Wong, C.H. Advances in glycoprotein synthesis. Chem. Commun. 21–33 (2006).
• Muir, T.W. Semisynthesis of proteins by expressed protein ligation. Annu. Rev. Biochem. 72, 249–289 (2003).
  Article CAS Google Scholar
• Saxon, E., Armstrong, J.I. & Bertozzi, C.R. A 'traceless' Staudinger ligation for the chemoselective synthesis of amide bonds. Org. Lett. 2, 2141–2143 (2000).
  Article CAS Google Scholar
• van Kasteren, S.I. et al. Expanding the diversity of chemical protein modification allows post-translational mimicry. Nature 446, 1105–1109 (2007).
  Article CAS Google Scholar
• Gamblin, D.P. et al. Glycosyl phenylthiosulfonates (Glyco-PTS): novel reagents for glycoprotein synthesis. Org. Biomol. Chem. 1, 3642–3644 (2003).
  Article CAS Google Scholar
• Gamblin, D.P. et al. Glyco-SeS: selenenylsulfide-mediated protein glycoconjugation—a new strategy in post-translational modification. Angew. Chem. Int. Ed. 43, 828–833 (2004).
  Article CAS Google Scholar
• Davis, B.G., Lloyd, R.C. & Jones, J.B. Controlled site-selective glycosylation of proteins by a combined site- directed mutagenesis and chemical modification approach. J. Org. Chem. 63, 9614–9615 (1998).
  Article CAS Google Scholar
• Hermanson, G.T. Bioconjugate Techniques 1st edn. (Academic Press, San Diego, California, 1996).
  Google Scholar
• Davis, B.G., Maughan, M.A.T., Green, M.P., Ullman, A. & Jones, J.B. Glycomethanethiosulfonates: powerful reagents for protein glycosylation. Tetrahedron Asymmetry 11, 245–262 (2000).
  Article CAS Google Scholar
• Swanwick, R.S., Daines, A.M., Flitsch, S.L. & Allemann, R.K. Synthesis of homogenous site-selectively glycosylated proteins. Org. Biomol. Chem. 3, 572–574 (2005).
  Article CAS Google Scholar
• MacMillan, D., Bill, R.M., Sage, K.A., Fern, D. & Flitsch, S.L. Selective in vitro glycosylation of recombinant proteins: semi-synthesis of novel homogeneous glycoforms of human erythropoietin. Chem. Biol. 8, 133–145 (2001).
  Article CAS Google Scholar
• Davis, B.G., Lloyd, R.C. & Jones, J.B. Controlled site-selective protein glycosylation for precise glycan structure-catalytic activity relationships. Bioorg. Med. Chem. 8, 1527–1535 (2000).
  Article CAS Google Scholar
• Tornøe, C.W., Christensen, C. & Meldal, M. Peptidotriazoles on solid phase: [1,2,3]-Triazoles by regiospecific copper(I)-catalyzed 1,3-dipolar cycloadditions of terminal alkynes to azides. J. Org. Chem. 67, 3057–3064 (2002).
  Article Google Scholar
• Demko, Z.P. & Sharpless, K.B. A click chemistry approach to tetrazoles by huisgen 1,3-dipolar cycloaddition: synthesis of 5-acyltetrazoles from azides and acyl cyanides. Angew. Chem. Int. Ed. 41, 2113–2116 (2002).
  Article CAS Google Scholar
• Kolb, H.C., Finn, M.G. & Sharpless, K.B. Click chemistry: diverse chemical function from a few good reactions. Angew. Chem. Int. Ed. 40, 2005–2021 (2001).
  Google Scholar
• Deiters, A. & Schultz, P.G. In vivo incorporation of an alkyne into proteins in Escherichia coli. Bioorg. Med. Chem. Lett. 15, 1521–1524 (2005).
  Article CAS Google Scholar
• Deiters, A. et al. Adding amino acids with novel reactivity to the genetic code of Saccharomyces cerevisiae. J. Am. Chem. Soc. 125, 11782–11783 (2003).
  Article CAS Google Scholar
• Lin, P.C. et al. Site-specific protein modification through Cu-I-catalyzed 1,2,3-triazole formation and its implementation in protein microarray fabrication. Angew. Chem. Int. Ed. 45, 4286–4290 (2006).
  Article CAS Google Scholar
• Yang, W., Hendrickson, W.A., Crouch, R.J. & Satow, Y. Structure of ribonuclease H phased at 2 A resolution by MAD analysis of the selenomethionyl protein. Science 249, 1398–1405 (1990).
  Article CAS Google Scholar
• Kiick, K.L., Weberskirch, R. & Tirrell, D.A. Identification of an expanded set of translationally active methionine analogues in Escherichia coli. FEBS Lett. 502, 25–30 (2001).
  Article CAS Google Scholar
• Kiick, K.L. & Tirrell, D.A. Protein engineering by in vivo incorporation of non-natural amino acids: control of incorporation of methionine analogues by methionyl-tRNA synthetase. Tetrahedron 56, 9487–9493 (2000).
  Article CAS Google Scholar
• Kiick, K.L., Saxon, E., Tirrell, D.A. & Bertozzi, C.R. Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation. Proc. Natl. Acad. Sci. USA 99, 19–24 (2002).
  Article CAS Google Scholar
• Kohler, G. & Milstein, C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 256, 495–497 (1975).
  Article CAS Google Scholar
• Bernardes, G.J., Gamblin, D.P. & Davis, B.G. The direct formation of glycosyl thiols from reducing sugars allows one-pot protein glycoconjugation. Angew. Chem. Int. Ed. 45, 4007–4011 (2006).
  Article CAS Google Scholar
• Bernardes, G.J. & Davis, B.G. Direct thionation of reducing sugars. Nat. Protoc. (2007) doi: 10.1038/nprot.2007.439.
• Drummer, O.H., Routley, L. & Christophidis, N. Reversibility of disulfide formation. Biochem. Pharmacol. 36, 1197–1201 (1987).
  Article CAS Google Scholar
• Lee, B. & Richards, F.M. The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55, 379–380 (1971).
  Article CAS Google Scholar
• Glocker, M.O., Borchers, C., Fiedler, W., Suckau, D. & Przybylski, M. Molecular characterization of surface topology in protein tertiary structures by amino-acylation and mass spectrometric peptide mapping. Bioconjug. Chem. 5, 583–590 (1994).
  Article CAS Google Scholar
• Stabile, M.R. et al. Probing the specificity of the S1 binding site of M222 mutants of subtilisin B. lentus with boronic acid inhibitors. Bioorg. Med. Chem. Lett. 6, 2501–2506 (1996).
  Article CAS Google Scholar
• Van Hest, J.C., Kiick, K.L. & Tirrell, D.A. Efficient incorporation of unsaturated methionine analogues into proteins in vivo. J. Am. Chem. Soc. 122, 1282–1288 (2000).
  Article CAS Google Scholar
• Perrin, D.D. & Armarego, W.L.F. Purification of Laboratory Chemicals (Pergamon Press, Oxford, 1988).
  Google Scholar
• Chan, T.R., Hilgraf, R., Sharpless, K.B. & Fokin, V.V. Polytriazoles as copper(I)-stabilizing ligands in catalysis. Org. Lett. 6, 2853–2855 (2004).
  Article CAS Google Scholar
• Bradford, M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72, 248–254 (1976).
  Article CAS Google Scholar