Taylor & Drickamer: Introduction to Glycobiology: 2e 
Key Reading References
Answers to ProblemsTaylor & Drickamer: Introduction to Glycobiology: 2e
Chapter 08
Key References:
Barondes, S.H., Cooper, D.N.W., Gitt, M.A., and Leffler, H. (1994) Galectins: structure and function of a large family of animal lectins. Journal of Biological Chemistry 269, 20807–20810. This paper provides an overview of the galectins, including details of crystal structures.
http://www.jbc.org/cgi/reprint/270/24/14243.pdf
Bleijs, D.A., Geijtenbeek, T.B.H., Figdor, C.G., and van Kooyk, Y. (2001) DC-SIGN and LFA-1: a battle for ligand. Trends in Immunology 22, 457–463. This is a short review of the evidence for a role of DC-SIGN in mediating adhesion of T cells to dendritic cells through binding to ICAM-2.
[You must have a username and password to access the full article at http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6W7H-43J6WW2-R-5&_cdi=6627&_user=126524&_orig=browse&_coverDate=08%2F01%2F2001&_sk=999779991&view=c&wchp=dGLbVzb-zSkWb&md5=ab3766248897dec3e8c39644b021cbe5&ie=/sdarticle.pdf]
Crocker, P.R. and Varki, A. (2001a) Siglecs in the immune system. Immunology 103, 137–145. This review, and Crocker and Varki (2001b) below, provide a good overview of the biochemistry and biology of the siglecs.
http://www.blackwell-synergy.com/doi/pdf/10.1046/j.0019-2805.2001.01241.x
Crocker, P.R. and Varki, A. (2001b) Siglecs, sialic acid and innate immunity. Trends in Immunology 22, 337–342.
[You must have a username and password to access the full article at http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6W7H-43N8BY5-W-7&_cdi=6627&_user=126524&_orig=browse&_coverDate=06%2F01%2F2001&_sk=999779993&view=c&wchp=dGLbVtb-zSkzk&md5=92c1b1faf7488d8e6039c9cf32bae040&ie=/sdarticle.pdf]
Cyster, J.G. and Goodnow, C.C. (1997) Tuning antigen receptor signaling by CD22: integrating cues from antigens and the microenvironment. Immunity 6, 509–517. This is a detailed review of the roles of CD22 in B cell signalling.
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Dwir, O., Kansas, G.S., and Alon, R. (2001) Cytoplasmic anchorage of L-selectin controls leukocyte capture and rolling by increasing the mechanical stability of the selectin tether. Journal ofCell Biology 155, 145–156. Experiments demonstrating the importance of interactions of the cytoplasmic domain of L-selectin with the cytoskeleton are described.
http://www.jcb.org/cgi/reprint/155/1/145.pdf
Epperson, T.K., Patel, K.D., McEver, R.P., and Cummings, R.D. (2000) Noncovalent association of P-selectin glycoprotein ligand-1 and minimal determinants for binding to P-selectin. Journal of Biological Chemistry 275, 7839–7853. Key experiments defining the interaction between P-selectin and its main physiological ligand are presented.
http://www.jbc.org/cgi/reprint/275/11/7839.pdf
Hemmerich, S. and Rosen, S.D. (2000) Carbohydrate sulfotransferases in lymphocyte homing. Glycobiology 10, 849–856. The roles of sulphated carbohydrates as selectin ligands and the sulphotransferases that synthesize them are reviewed.
http://glycob.oxfordjournals.org/cgi/reprint/13/4/245.pdf
Hernandez, J.D. and Baum L.G. (2002) Ah, sweet mystery of death! Galectins and control of cell fate. Glycobiology 12, 127R-136R. A detailed review of the evidence that galectins are involved in apoptosis.
http://glycob.oxfordjournals.org/cgi/reprint/12/10/127R.pdf
Hu, Y., Szente, B., Kiely, J.-M., and Gimbrone, M.A., Jr. (2001) Molecular events in transmembrane signaling via E-selectin. SHP2 association, adapter protein complex formation and ERK1/2 activation. Journal of Biological Chemistry 276, 48549–48553. Experiments demonstrating that outside-in signalling by E-selectin requires association of the cytoplasmic domain of E-selectin with a tyrosine phosphatase are presented.
http://www.jbc.org/cgi/reprint/276/51/48549.pdf
Hughes, R.C. (2001) Galectins as modulators of cell adhesion. Biochimie 83, 667–676. This paper provides a detailed and critical review of the structures and functions of the galectins.
[You must have a username and password to access the full article at http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6VRJ-445Y8RK-H-9&_cdi=6236&_user=126524&_orig=browse&_coverDate=07%2F31%2F2001&_sk=999169992&view=c&wchp=dGLbVlz-zSkWA&md5=d9acbc63af71ad52540c0a2399d91eae&ie=/sdarticle.pdf]
Lübke, T., Marquardt, T., Etzioni, A., Hartmann, E., von Figura, K., and Körner, C. (2001) Complementation cloning identifies CDG-IIc, a new type of congenital disorder of glycosylation, as a GDP-fucose transporter deficiency. Nature Genetics 28, 73–76. This paper, and Lühn et al. (2001, see below), describe determination of the molecular basis for leucocyte adhesion deficiency II.
http://www.nature.com/ng/journal/v28/n1/pdf/ng0501_73.pdf
Lühn, K., Wild, M.K., Eckhardt, M., Gerardy-Schahn, R., and Vestweber, D. (2001) The gene defective in leukocyte adhesion deficiency II encodes a putative GDP-fucose transporter. Nature Genetics 28, 69–72.
http://www.nature.com/ng/journal/v28/n1/pdf/ng0501_69.pdf
May, A.P., Robinson, R.C., Vinson, M., Crocker, P.R., and Jones, E.Y. (1998) Crystal structure of the N-terminal domain of sialoadhesin in comples with 3 ¢ -sialyllactose at 1.85 Å resolution. Molecular Cell 1, 719–728. The molecular basis for sialic acid binding by I-type CRDs of the siglecs is presented.
http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6WSR-4194JH5-9-M&_cdi=7053&_user=126524&_orig=browse&_coverDate=04%2F30%2F1998&_sk=999989994&view=c&wchp=dGLbVtb-zSkWb&md5=8ad669f54aedf9f49b04e9d6cf8afdcb&ie=/sdarticle.pdf
Pohlmann, S., Baribaud, F., and Doms, R.W. (2001) DC-SIGN and DC-SIGNR: helping hands for HIV. Trends in Immunology 22, 643–646. The evidence for roles of DC-SIGN and DC-SIGNR in facilitating HIV infection of T cells is reviewed.
[You must have a username and password to access the full article at http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6W7H-44K9FFW-1-5&_cdi=6627&_user=126524&_orig=browse&_coverDate=12%2F01%2F2001&_sk=999779987&view=c&wchp=dGLbVzz-zSkWW&md5=68e4192956c4263d7054f46ee0b141a3&ie=/sdarticle.pdf]
Powell, L.D. and Varki, A. (1995) I-type lectins. Journal of Biological Chemistry 270, 14243–14246. This is a short review covering the siglecs, with particular reference to CD22, and other potential I-type lectins.
http://www.jbc.org/cgi/reprint/270/24/14243.pdf
Rini, J.M. (1995) Lectin structure. Annual Review of Biophysics and Biomolecular Structure 24, 551–577. This paper, and Weis and Drickamer (1996, see below), provide detailed reviews of animal lectin structures determined by crystallography, and the principles underlying protein–carbohydrate interactions.
[Your institution will need to be a subscriber to access this article online at: http://arjournals.annualreviews.org/doi/pdf/10.1146/annurev.bb.24.060195.003003]
Somers, W.S., Tang, J., Shaw, G.D., and Camphausen, R.T. (2000) Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to SLe X and PSGL-1. Cell 103, 467–479. Crystal structures of the C-type CRDs of two selectins in complex with sialyl Lewis X are described.
http://download.cell.com/pdfs/0092-8674/PIIS0092867400001380.pdf
Stahl, P.D. and Ezekowitz, R.A.B. (1998) The mannose receptor is a pattern recognition receptor involved in host defense. Current Opinion in Immunology 10, 50–55. This paper provides an overview of the properties of the mannose receptor and its possible functions in the immune system.
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Steinman, R.M. (2000) DC-SIGN: a guide to some mysteries of dendritic cells. Cell 100, 491–494. This short commentary provides a good introduction to the functions of dendritic cells in the immune system and the possible roles of DC-SIGN.
http://download.cell.com/pdfs/0092-8674/PIIS0092867400806844.pdf
Turner, M.W. (1996) Mannose-binding lectin: the pluripotent molecule of the innate immune system. Immunology Today17, 532–540. This paper provides an overview of the properties of mannose-binding protein and its functions in the immune system. Not available online.
van der Merwe, P.A. (1999) Leukocyte adhesion: high-speed cells with ABS. Current Biology 9, R419–R422. The kinetic properties of selectin–ligand interactions in leucocyte adhesion are reviewed.
http://download.current-biology.com/pdfs/0960-9822/PIIS0960982299802589.pdf
van Kooyk, Y. and Geijtenbeek, T.B.H. (2003) DC-SIGN: escape mechanism for pathogens. Nature Reviews Immunology 3, 697-709. This review gives details of the interactions of DC-SIGN with pathogenic micro-organisms.
[Your institution will need to be a subscriber to access this article online at: http://www.nature.com/nri/journal/v3/n9/pdf/nri1182.pdf]
Vestweber, D. and Blanks, J.E. (1999) Mechanisms that regulate the function of selectins and their ligands. Physiological Reviews 79, 181–213. This is a detailed review of the selectins.
http://physrev.physiology.org/cgi/reprint/79/1/181.pdf
Wallis, R., Shaw, J.M., Uitdehaag, J., Chen, C.-B., Torgersen, D. and Drickamer, K. (2004) Localization of the serine protease-binding sites in the collagen-like domain of mannose-binding protein: indirect effects of naturally occurring mutations on protease binding and activation. Journal of Biological Chemistry 279, 14065-14073. Key experiments that show the molecular basis for the immunodeficiency caused by mutations in human mannose-binding protein are presented.
http://www.jbc.org/cgi/reprint/279/14/14065.pdf
Weis, W.I. and Drickamer, K. (1996) Structural basis of lectin-carbohydrate interaction. Annual Review of Biochemistry 65, 441–473.
http://arjournals.annualreviews.org/doi/pdf/10.1146/annurev.bi.65.070196.002301
Weis, W.I., Taylor, M.E., and Drickamer, K. (1998) The C-type lectin superfamily in the immune system. Immunological Reviews 163, 19–34. The structures and functions of C-type lectins with roles in the immune system are reviewed. Mannose-binding protein, other collectins, the mannose receptor, and the selectins, as well as C-type lectin-like proteins on natural killer cells are included. Not available online.
Questions
2) Go to the genomic resource for animal lectins at http://www.imperial.ac.uk/research/animallectins/. In the C-type lectin-like domain (CTLD) database, first look at the domain organization of mammalian proteins containing CTLDs, then examine the sequences of the CTLDs in group II (type II receptors) and group V (NK receptors). Discuss why some of these receptors are not predicted to bind sugars, while others would be expected to bind either mannose or galactose.
References:
Weis, W.I., Drickamer, K. and Hendrickson, W.A. (1992) Structure of a C-type mannose-binding protein complexed with an oligosaccharide. Nature 360, 127-134. Not available online.
Drickamer, K. (1992) Engineering galactose-binding activity into a C-type mannose-binding protein. Nature 360, 183-186. Not available online.
4) Describe some of the approaches that have been used to identify glycoprotein ligands for the selectins.
Lead References:
Fieger, C.B., Sassetti, C.M. and Rosen, S.D. (2003) Endoglycan, a member of the CD34 family, functions as an L-selectin ligand through modification with tyrosine sulfation and sialyl Lewis x. Journal of Biological Chemistry 278, 27390-27398.
http://www.jbc.org/cgi/reprint/278/30/27390.pdf
Levinovitz, A., Muhlhoff, J., Isenmann, S. and Vestweber, D. (1993) Identification of a glycoprotein ligand for E-selectin on mouse myeloid cells. Journal of Cell Biology 121, 449-459.
http://www.jcb.org/cgi/reprint/121/2/449.pdf
6) No clear function for sialoadhesin has so far been determined although it is thought to be involved in adhesion interactions of macrophages. Discuss how the experiments presented in the following paper provide evidence that sialoadhesin might function as a pathogen receptor.
Reference:
Jones, C., Virji, M. and Crocker, P. (2003) Recognition of sialylated meningococcal lipopolysaccharide by siglecs expressed on myeloid cells leads to enhanced bacterial uptake. Molecular Microbiology 49, 1213-1225
http://www.blackwell-synergy.com/production/cmi/2004/6/7/j.1462-5822.2004.00387.x/j.1462-5822.2004.00387.x.pdf?sessionID=bM00Kb_O9wh7agKMBI
Box 8.1 Glycotherapeutics: Drugs and antibodies that prevent HIV infection mimic recognition by DC-SIGN
Lead references:
Botos, I. and Wlodawer, A. (2003) Cyanovirin-N: a sugar-binding antiviral protein with a new twist. Cellular and Molecular Life Sciences 60, 277-287.
http://www.springerlink.com/media/159pujryum5317hp9g7t/contributions/6/g/m/9/6gm96ux7vkhva558.pdf
Barrientos, L.G., Lasala, F., Delgado, R., Sanchez, A. and Gronenborn, A.M. (2004) Flipping the switch from monomeric to dimeric CV-N has little effect on antiviral activity. Structure 12, 1799-1807.
[You must have a username and password to access the full article at http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6VSR-4DGCDM1-7-D&_cdi=6269&_user=217827&_orig=search&_coverDate=10%2F31%2F2004&_qd=1&_sk=999879989&view=c&wchp=dGLbVlb-zSkWz&md5=35db225ace4f97b4fb6c573d9b0e20ac&ie=/sdarticle.pdf]
Tsai, C.-C., Emau, P., Jiang, Y., Agy, M.B., Shattock, R.J., Schmidt, A., Morton, W.R., Gustafson, K.R. and Boyd, M.R. (2004) Cyanovirin-N inhibits AIDS virus infection in vaginal transmission models. AIDS Research and. Human Retroviruses 20, 11-18.
http://www.liebertonline.com/doi/pdf/10.1089/088922204322749459;jsessionid=o4U9D8b2n7Jdj_xmFI
Calarese, D.A., Scanlan, C.N., Zwick, M.B., Deechongkit, S., Mimura, Y., Kunert, R., Zhu, P., Wormald, M.R., Stanfield, R.L., Roux, K.H., Kelly, J.W., Rudd, P.M., Dwek, R.A., Katinger, H., Burton, D.R. and Wilson, I.A. (2003) Antibody domain exchange is an immunological solution to carbohydrate cluster recognition. Science 300, 2065-2071.
http://www.sciencemag.org/cgi/reprint/300/5628/2065.pdf
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