Taylor & Drickamer: Introduction to Glycobiology: 2e 
Key Reading References
Answers to ProblemsTaylor & Drickamer: Introduction to Glycobiology: 2e
Chapter 10
Key References:
Bouckaert, J., Hamelryck, T., Wyns, L., and Loris, R. (1999) Novel structures of plant lectins and their complexes with carbohydrates. Current Opinion in Structural Biology 9, 572–577. An overview of the structural basis for carbohydrate recognition by different types of plant lectin is provided.
[You must have a username and password to access the full article at http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6VS6-3Y6XCHB-7-9&_cdi=6254&_user=217827&_orig=browse&_coverDate=10%2F01%2F1999&_sk=999909994&view=c&wchp=dGLbVlz-zSkWz&md5=e3438dd56fc42cd524500521e6d9a980&ie=/sdarticle.pdf]
Burnette, W.N. (1994) AB5 ADP-ribosylating toxins: comparative anatomy and physiology. Structure 2, 151–158. This paper provides an overview of these carbohydrate-binding bacterial toxins, including details of crystal structures.
[You must have a username and password to access the full article at http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6VSR-4D1KWTK-H-3&_cdi=6269&_user=217827&_orig=search&_coverDate=03%2F31%2F1994&_qd=1&_sk=999979996&view=c&wchp=dGLbVtz-zSkWW&md5=8e700e2d016bc0b1fa1abe66c2b76494&ie=/sdarticle.pdf]
Day, P.J., Owens, S.R., Wesche, J., Olsnes, S., Roberts, L.M., and Lord, J.M. (2001) An interaction between ricin and calreticulin that may have implications for toxin trafficking. Journal of Biological Chemistry 276, 7202–7208. Experiments demonstrating that calreticulin acts as a carrier for ricin during retrograde transport to the endoplasmic reticulum are described.
http://www.jbc.org/cgi/reprint/276/10/7202.pdf
Dodd, R.B. and Drickamer, K. (2000) Lectin-like proteins in model organisms: implications for evolution of carbohydrate-binding activity. Glycobiology 11, 71R–79R. A comparative analysis of lectins identified in the genomes of yeast, Drosophila, and Caenorhabditis elegans is presented.
http://glycob.oxfordjournals.org/cgi/reprint/11/5/71R.pdf
Dodson, K.W., Pinkner, J.S., Rose, T., Magnusson, G., Hultgren, S.J., and Waksman, G. (2001) Structural basis of the interaction of the pyelonephritic E. coli adhesin to its human kidney receptor. Cell 105, 733–743. Analysis of the crystal structure of PapG in complex with its globoside ligand, providing insights into this host-pathogen interaction is described.
http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6WSN-4C5GRC4-7-P&_cdi=7051&_user=217827&_orig=search&_coverDate=06%2F15%2F2001&_qd=1&_sk=998949993&view=c&wchp=dGLbVtb-zSkWW&md5=0de6a5ff8a425cf8f1992eb55dfbff63&ie=/sdarticle.pdf
Lis, H. and Sharon, N. (1998) Lectins: carbohydrate-specific proteins that mediate cellular recognition. Chemical Reviews 98, 637–674. This is an extensive review of lectins including a wealth of detail on lectins from plants and micro-organisms.
[Your institution will need to be a subscriber to access this article online at: http://pubs.acs.org/cgi-bin/article.cgi/chreay/1998/98/i02/pdf/cr940413g.pdf]
Lord, J.M. and Roberts, L.M. (1998) Retrograde transport: going against the flow. Current Biology 8, R56–R58. This is a short commentary on transport from the Golgi back to the endoplasmic reticulum.
http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6VRT-4CXMMBW-C-5&_cdi=6243&_user=217827&_orig=search&_coverDate=01%2F15%2F1998&_qd=1&_sk=999919997&view=c&wchp=dGLbVlb-zSkWb&md5=b8145fc48f526137ca3859a4957c170b&ie=/sdarticle.pdf
Promé, J.-C. (1996) Signalling events elicited in plants by defined oligosaccharide structures. Current Opinion in Structural Biology 6, 671–678. This is a detailed review of how plants use oligosaccharides as signalling molecules.
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Sandvig, K. and van Deurs, B. (2000) Entry of ricin and Shiga toxin into cells: molecular mechanisms and medical perspectives. EMBO Journal 19, 5943–5950. This is a detailed review of the mechanism of action of these two carbohydrate-binding toxins.
http://www.nature.com/emboj/journal/v19/n22/pdf/7593408a.pdf
Sauer, F.G., Barnhart, M., Choudhury, D., Knight, S.D., Waksman, G., and Hultgren, S.J. (2000) Chaperone-assisted pilus assembly and bacterial attachment. Current Opinion in Structural Biology 10, 548–556. The structure and function of adhesins of bacterial pili are reviewed in detail.
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Sixma, T.K., Pronk, S.E., Kalk, K.H., van Zanten, B.A.M., Berghuis, A.M., and Hol, W.G.J. (1992) Lactose binding to heat-labile enterotoxin revealed by X-ray crystallography. Nature 355, 561–564. The structural basis for carbohydrate recognition by this bacterial toxin is described. The structural basis for carbohydrate recognition by this bacterial toxin is described. Not available online.
Steeves, R.M., Denton, M.E., Barnard, F.C., Henry, A., and Lambert, J.M. (1999) Identification of three oligosaccharide binding sites in ricin. Biochemistry 38, 11677–11685. Affinity labelling studies of ricin are presented.
[Your institution will need to be a subscriber to access this article online at: http://pubs.acs.org/cgi-bin/article.cgi/bichaw/1999/38/i36/pdf/bi990493o.pdf]
Wade, R.C. (1997) ‘Flu’ and structure-based drug design. Structure 5, 1139–1145. This paper gives an overview of structural studies on influenza haemagglutinin and neuraminidase, and the attempts to design inhibitors of their interactions with host cell surface glycans.
http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6VSR-4CJB90S-82-C&_cdi=6269&_user=217827&_orig=search&_coverDate=09%2F15%2F1997&_qd=1&_sk=999949990&view=c&wchp=dGLbVzz-zSkWb&md5=e7bceef57d4d86788975f40247d08308&ie=/sdarticle.pdf
Watowich, S.J., Skehel, J.J., and Wiley, D.C. (1994) Crystal structures of influenza virus hemagglutinin in complex with high-affinity receptor analogs. Structure 2, 719–731. Analysis of the structural basis for sialic acid recognition by influenza haemagglutinin is presented.
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Questions
2) Recent studies have shown that protein glycosylation occurs in some species of bacteria. What is known about N-linked glycosylation in Campylobacter and how does it compare to N-linked glycosylation in eukaryotes?
References:
Linton, D., Dorrell, N., Hitchen, P.G., Amber, S., Karlyshev, A.V., Morris, H.R., Dell, A., Wren, A.B. and Aebi, M. (2005) Functional analysis of the Campylobacter jejuni N-linked protein glycosylation pathway. Molecular Microbiology 55, 1695-1703.
[Your institution will need to be a subscriber to access this article online at: http://www.blackwell-synergy.com/doi/full/10.1111/j.1365-2958.2005.04519.x]
Wacker, M., Linton, D., Hitchen, P.G., Nita-Lazar, M., Haslam, S.M., North, S.J., Morris, H.R., Dell, A., Wren, A.B. and Aebi, M. (2002) N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli. Science 298, 1790-1793.
[Your institution will need to be a subscriber to access this article online at: http://www.sciencemag.org/cgi/reprint/298/5599/1790.pdf]
Szymanski, C.M., Logan, S.M., Linton, D. and Wren, B.W. (2003) Campylobacter -- a tale of two protein glycosylation systems. Trends in Microbiology 11, 233-238.
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3) Discuss how studies of the interactions of influenza haemagglutinin and neuraminidase with carbohydrates have been useful in attempts to design anti-influenza drugs.
Lead reference:
Wade, R.C. (1997) ‘Flu’ and structure-based drug design. Structure 5, 1139–1145.
http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6VSR-4CJB90S-82-C&_cdi=6269&_user=217827&_orig=search&_coverDate=09%2F15%2F1997&_qd=1&_sk=999949990&view=c&wchp=dGLbVzz-zSkWb&md5=e7bceef57d4d86788975f40247d08308&ie=/sdarticle.pdf
4) Transgenic plants are attractive as hosts for producing recombinant glycoproteins. Discuss why the glycosylation produced by plant cells might not be suitable for therapeutic glycoproteins and what can be done to overcome this problem.
Lead reference:
Strasser, R., Altmann, F., Mach, L., Glossl, J. and Steinkellner, H. (2004) Generation of Arabidopsis thaliana plants with complex N-glycans lacking beta1,2-linked xylose and core alpha1,3-linked fucose. FEBS letters 561, 132-136.
http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6T36-4BRT3RV-1-7&_cdi=4938&_user=217827&_orig=search&_coverDate=03%2F12%2F2004&_qd=1&_sk=994389998&view=c&wchp=dGLbVtb-zSkzV&md5=4f39e148786dd77189b710c3a8182b4d&ie=/sdarticle.pdf
Box 10.1 Glycotherapeutics: Glycobiology of Disease: Bacteria that cause stomach ulcers use blood group glycans as receptors
Lead references:
Karlsson, K.-A. (2000) The human gastric colonizer Helicobacter pylori: a challenge for host-parasite glycobiology. Glycobiology 10, 761-771.
http://glycob.oxfordjournals.org/cgi/reprint/10/8/761.pdf
Ilver, D., Arnqvist, A., Ögren, J., Frick, I.-M., Kersulyte, D., Incecik, E.T., Berg, D.E., Covacci, A., Engstrand, L. and Borén, T. (1998) Helicobacter pyloriadhesin binding fucosylated histo-blood group antigens revealed by retagging. Science 279, 373-377.
[Your institution will need to be a subscriber to access this article online at: http://www.sciencemag.org/cgi/reprint/279/5349/373.pdf]
Mahdavi, J., Sondén, B., Hurtig, M., Olfat, F.O., Forsberg, L., Roche, N. Ångström, J., Larsson, T., Teneberg, S., Karlsson, K.-A., Altraja, S., Wadström, T., Kersulyte, D., Berg, D.E., Dubois, A., Petersson, C., Magnusson, K.-E., Norberg, T., Lindh, F., Lundskog, B.B., Arnqvist. A., Hammarström, L. and Borén, T. (2002) Helicobacter pylori SabA adhesin in persistent infection and chronic inflammation. Science 297, 573-578.
[Your institution will need to be a subscriber to access this article online at: http://www.sciencemag.org/cgi/reprint/297/5581/573.pdf]
Bergmann, M.P., Engering, A., Smits, H.H., van Vliet, S.J., van Bodegraven, A.A., Wirth, H.-P., Kapsenberg, M.L., Vandenbroucke-Grauls, C.M.J.E., van Kooyk, Y. and Appelmelk, B.J. (2004) Helicobacter pylori modulates the T helper cell 1/T helper cell 2 balance through phase-variable interactions between lipopolysaccharide and DC-SIGN. Journal of Experimental Medicine 200, 979-990.
http://www.jem.org/cgi/reprint/200/8/979.pdf
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