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Taylor & Drickamer: Introduction to Glycobiology: 2e

Chapter 07

Key References:

Blum, M.L., Down, J.A., Gurnett, A.M., Carrington, M., Turner, M.J., and Wiley, D.C. (1993) A structural motif in the variant surface glycoproteins of Trypanosoma brucei. Nature 362, 603–609. In this paper, crystallographic analysis of the structures of two trypanosome variant surface glycoproteins is presented. Not available online.

Delorme, E., Lorenzini, T., Griffin, J., Martin, F., Jacobsen, F., Boone, T., and Elliott, S. (1992) Role of glycosylation on the secretion and biological activity of erythropoietin. Biochemistry 31, 9871–9876. An analysis of the importance of N- and O-linked glycans of erythropoietin by site-directed mutagenesis and functional assays is described.
http://pubs.acs.org/cgi-bin/archive.cgi/bichaw/1992/31/i41/pdf/bi00156a003.pdf

Dwek, R.A. (1995) Glycobiology: towards understanding the function of sugars. Biochemical SocietyTransactions 23, 1–25. Some key examples of how glycosylation affects protein function are reviewed. Not available online.

Mer, G., Hietter, H., and Lefevre, J.-F. (1996) Stabilization of proteins by glycosylation examined by NMR analysis of a fucosylated proteinase inhibitor. Nature Structural Biology 3, 45–53. The experiments showing stabilization of the proteinase inhibitor PMP-C by O-linked fucose are described.
[Your institution will need to be a subscriber to access this article online at: http://www.nature.com/nsmb/journal/v3/n1/pdf/nsb0196-45.pdf]

Purohit, S., Shao, K., Balasubramanian, S.V., and Bahl, O.P. (1997) Mutants of human choriogonadotropin lacking N-glycosyl chains in the a -subunit: mechanism for the differential action of the N-linked carbohydrates. Biochemistry 36, 12355–12363. This paper describes analysis of the effects of N-linked glycans of choriogonadotrophin on structure and activity of the hormone.
[Your institution will need to be a subscriber to access this article online at: http://pubs.acs.org/cgi-bin/archive.cgi/bichaw/1997/36/i40/pdf/bi970303e.pdf]

Wittwer, A. and Howard, S.C. (1990) Glycosylation at Asn-184 inhibits the conversion of single-chain tissue-type plasminogen activator by plasmin. Biochemistry 29, 4175–4180. Key experiments showing that glycosylation modulates tPA activity by inhibiting proteolysis are presented.
[Your institution will need to be a subscriber to access this article online at: http://pubs.acs.org/cgi-bin/archive.cgi/bichaw/1990/29/i17/pdf/bi00469a021.pdf]

Wormald, M.R. and Dwek, R.A. (1999) Glycoproteins: glycan presentation and protein-fold stability. Structure 7, R155–R160. Several examples of proteins stabilized by the presence of N-linked glycans are reviewed.
http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6VSR-3XBTS7X-1-1&_cdi=6269&_user=126524&_orig=search&_coverDate=07%2F15%2F1999&_qd=1&_sk=999929992&view=c&wchp=dGLzVlz-zSkzk&md5=6f1a3383353534d1a7731632882b4380&ie=/sdarticle.pdf

Wyss, D.F., Choi, J.S., Li, J., Knoppers, M.H., Willis, K.J., Arulanandam, A.R.N., Smolyar, A., Reinherz, E.L., and Wagner, G. (1995) Conformation and function of the N-linked glycan in the cell adhesion domain of human CD2. Science 269, 1273–1278. Experiments showing that CD2 is stabilized by a high mannose N-linked oligosaccharide are described. Not available online.

Questions

3) Discuss the experiments used to show that N-linked oligosaccharides protect some lysosomal membrane proteins from proteolysis.

Reference: Kundra, R. and Kornfeld, S. (1999) Asparagine-linked oligosaccharides protect Lamp-1 and Lamp-2 from intracellular proteolysis. Journal of Biological Chemistry 274, 31039-31046.
http://www.jbc.org/cgi/reprint/274/43/31039.pdf

4) How does glycosylation of the IgG Fc region affect its function?

References: Radaev, S. and Sun, P.D. (2001) Recognition of IgG Fcγ receptor: The role of Fc glycosylation and the binding of peptide inhibitors. Journal of Biological Chemistry 276, 16478-16483.
http://www.jbc.org/cgi/reprint/276/19/16478.pdf

Radaev, S., Motyka, S., Fridman, W.-H., Sautes-Fridman, C. and Sun, P.D. (2001) The structure of a human type III Fcγ receptor in complex with Fc. Journal of Biological Chemistry 276, 16469-16477.
http://www.jbc.org/cgi/reprint/276/19/16469.pdf

Box 5 Glycobiology and disease: Differential glycosylation of prion proteins may be linked to the conformational changes leading to CJD and related diseases.
Lead references:

Lawson, V.A., Collins, S.J., Masters, C.L. and Hill, A.F. (2005) Prion protein glycosylation. Journal of Neurochemistry 93, 793-801.
http://www.blackwell-synergy.com/doi/pdf/10.1111/j.1471-4159.2005.03104.x

Collinge, J., Sidle, K.C.L., Meads, J., Ironside, J. and Hill, A.F. (1996) Molecular analysis of prion strain variation and the aetiology of “new variant” CJD. Nature 383, 685-690. Not available online.

Rudd, P.M., Endo, T., Colominas, C., Groth, D., Wheeler, S.F., Harvey, D.J., Wormald, M.R., Serban, H., Prusiner, S.B., Kobata, A. and Dwek, R.A. (1999) Glycosylation differences between the normal and pathogenic prion protein isoforms. Proceedings of the National Academy of Sciences USA 96, 13044-13049.
http://www.pnas.org/cgi/reprint/96/23/13044.pdf

Hornemann, S., Schorn, C. and Wutrich, K. (2005) NMR structure of the bovine prion protein isolated from healthy calf brains. EMBO reports 5, 1159-1164.
[Your institution will need to be a subscriber to access this article online at: http://www.nature.com/embor/journal/v5/n12/pdf/7400297.pdf]