Disease-associated carbohydrate-recognising proteins and structure-based inhibitor design

Current Opinion in Structural Biology

Volumn 18, Issue 5, 2008, Pages 558-566

  von Itzstein, Mark ^a  

^a GRIFFITH UNIVERSITY   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

2 AMINOTHIAZOLE DERIVATIVE; 2 DEOXY 2,3 DIDEHYDROACETYLNEURAMINIC ACID; 4 ACETAMIDO 5 AMINO 3 (1 ETHYLPROPOXY) 1 CYCLOHEXENE 1 CARBOXYLIC ACID; 4 THIAZOLIDINONE DERIVATIVE; ANTIFUNGAL AGENT; ANTIINFECTIVE AGENT; ANTIINFLAMMATORY AGENT; ANTINEOPLASTIC AGENT; ANTIPROTOZOAL AGENT; ANTITRYPANOSOMAL AGENT; ANTIVIRUS AGENT; BAMBERMYCIN; CARBOHYDRATE RECOGNIZING PROTEIN; ENZYME INHIBITOR; ETHAMBUTOL; GALECTIN; INFLUENZA VIRUS HEMAGGLUTININ; LECTIN; PROTEIN DERIVATIVE; PROTEIN INHIBITOR; RIFAMPICIN; TUBERCULOSTATIC AGENT; UNCLASSIFIED DRUG; URIDINE TRIPHOSPHATE GLUCOSE 1 PHOSPHATE URIDYLYLTRANSFERASE; VIRUS SIALIDASE;

ANTIBIOTIC RESISTANCE; APOPTOSIS; AUTOIMMUNITY; CANCER GROWTH; CHAGAS DISEASE; DIABETES MELLITUS; DISEASE ASSOCIATION; DRUG DESIGN; DRUG MECHANISM; DRUG POTENCY; DRUG PROTEIN BINDING; DRUG TARGETING; HUMAN; INBORN ERROR OF METABOLISM; INFANTILE GASTROENTERITIS; INFLAMMATION; INFLUENZA VIRUS A H5N1; KLEBSIELLA PNEUMONIAE; LEISHMANIA MAJOR; LOWER RESPIRATORY TRACT INFECTION; MOLECULAR RECOGNITION; MYCOBACTERIUM; MYCOBACTERIUM TUBERCULOSIS; NEOPLASM; NONHUMAN; PARAINFLUENZA VIRUS; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTEIN TARGETING; REVIEW; ROTAVIRUS; SACCHAROMYCES CEREVISIAE; STAPHYLOCOCCUS AUREUS; TRYPANOSOMA CRUZI; TUBERCULOSIS; UPPER RESPIRATORY TRACT INFECTION;

ANIMALS; ANTI-BACTERIAL AGENTS; ANTIFUNGAL AGENTS; ANTIVIRAL AGENTS; CHAGAS DISEASE; DRUG DESIGN; DRUG RESISTANCE, MULTIPLE; HEMAGGLUTININS; HUMANS; INTRAMOLECULAR TRANSFERASES; MYCOBACTERIUM TUBERCULOSIS; NEURAMINIDASE; STAPHYLOCOCCUS AUREUS; TRYPANOCIDAL AGENTS; TRYPANOSOMA CRUZI;

AVIAN INFLUENZA VIRUS; ORTHOMYXOVIRIDAE;

EID: 53249098393     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2008.07.006     Document Type: Review

References (69)

1. Lovering A.L., de Castro L.H., Lim D., and Strynadka N.C.J. Structural insight into the transglycosylation step of bacterial cell-wall biosynthesis. Science 315 (2007) 1402-1405. The structural description of an essential enzyme in the biosynthesis of the bacterial cell wall.
2. Sun H.Y., Lin S.W., Ko T.P., Pan J.F., Liu C.L., Lin C.N., Wang A.H.J., and Lin C.H. Structure and mechanism of Helicobacter pylori fucosyltransferase. A basis for lipopolysaccharide variation and inhibitor design. J Biol Chem 282 (2007) 9973-9982
3. Yuan Y., Barrett D., Zhang Y., Kahne D., Sliz P., and Walker S. Crystal structure of a peptidoglycan glycosyltransferase suggests a model for processive glycan chain synthesis. Proc Nat Acad Sci 104 (2007) 5348-5353
4. World Health Organisation. Fact Sheet No. 104 (2002), World Health Organisation, Geneva
5. de Lederkremer R.M., and Colli W. Galactofuranose-containing glycoconjugates in trypanosomatids. Glycobiology 5 (1995) 547-552
6. Yuan Y., Bleile D.W., Wen X., Sanders D.A.R., Itoh K., Liu H.W., and Pinto B.M. Investigation of binding of UDP-Galf and UDP-[3-F]Galf to UDP-galactopyranose mutase by STD-NMR spectroscopy, molecular dynamics, and CORCEMA-ST calculations. J Am Chem Soc 130 (2008) 3157-3168
7. Dykhuizen E.C., May J.F., Tongpenyai A., and Kiessling L.L. Inhibitors of UDP-galactopyranose mutase thwart mycobacterial growth. J Am Chem Soc 130 (2008) 6706-6707
8. Davis C.B., Hartnell R.D., Madge P.D., Owen D.J., Thomson R.J., Chong A.K., Coppel R.L., and von Itzstein M. Synthesis and biological evaluation of galactofuranosyl alkyl thioglycosides as inhibitors of mycobacteria. Carbohydr Res 342 (2007) 1773-1780
9. Owen D.J., Davis C.B., Hartnell R.D., Madge P.D., Thomson R.J., Chong A.K., Coppel R.L., and von Itzstein M. Synthesis and evaluation of galactofuranosyl N,N-dialkyl sulfenamides and sulfonamides as antimycobacterial agents. Bioorg Med Chem Lett 17 (2007) 2274-2277
10. von Itzstein M., Plebanski M., Cooke B.M., and Coppel R.L. Hot, sweet and sticky: the glycobiology of Plasmodium falciparum. Trends Parasitol 24 (2008) 210-218. The authors provide an overview of the important carbohydrate-related pathways associated with P. falciparum.
11. Fan E., Baker D., Fields S., Gelb M.H., Buckner F.S., Van Voorhis W.C., Phizicky E., Dumont M., Mehlin C., Grayhack E., et al. Structural genomics of pathogenic protozoa: an overview. Methods Mol Biol 426 (2008) 497-513
12. Gayathri P., Balaram H., and Murthy M.R. Structural biology of plasmodial proteins. Curr Opin Struct Biol 17 (2007) 744-754
13. Steiner T., Lamerz A.C., Hess P., Breithaupt C., Krapp S., Bourenkov G., Huber R., Gerardy-Schahn R., and Jacob U. Open and closed structures of the UDP-glucose pyrophosphorylase from Leishmania major. J Biol Chem 282 (2007) 13003-13010
14. Buchini S., Buschiazzo A., and Withers S.G. A new generation of specific Trypanosoma cruzi trans-sialidase inhibitors. Angew Chem Int Ed Engl 47 (2008) 2700-2703. The authors describe the synthesis, biological and structural evaluation of a N-acetylneuraminic acid-based inhibitor of trans-sialidase.
15. Teixeira A.R., Nitz N., Guimaro M.C., Gomes C., and Santos-Buch C.A. Chagas disease. Postgrad Med J 82 (2006) 788-798
16. Buscaglia C.A., Campo V.A., Frasch A.C., and Di Noia J.M. Trypanosoma cruzi surface mucins: host-dependent coat diversity. Nat Rev Microbiol 4 (2006) 229-236
17. Ruge E., Korting H.C., and Borelli C. Current state of three-dimensional characterisation of antifungal targets and its use for molecular modelling in drug design. Int J Antimicrob Agents 26 (2005) 427-441
18. Hurtado-Guerrero R., and van Aalten D.M. Structure of Saccharomyces cerevisiae Chitinase 1 and screening-based discovery of potent inhibitors. Chem Biol 14 (2007) 589-599
19. de Jong M.D., and Hien T.T. Avian influenza A (H5N1). J Clin Virol 35 (2006) 2-13
20. von Itzstein M. The war against influenza: discovery and development of sialidase inhibitors. Nat Rev Drug Discov 6 (2007) 967-974. An overview of the discovery of influenza virus sialidase inhibitors.
21. Reece P.A. Neuraminidase inhibitor resistance in influenza viruses. J Med Virol 79 (2007) 1577-1586
22. Yang Y., Halloran M.E., Sugimoto J., and Longini Jr. I.M. Detecting human-to-human transmission of avian influenza A (H5N1). Emerg Infect Dis 13 (2007) 1348-1353
23. Collins P.J., Haire L.F., Lin Y.P., Liu J., Russell R.J., Walker P.A., Skehel J.J., Martin S.R., Hay A.J., and Gamblin S.J. Crystal structures of oseltamivir-resistant influenza virus neuraminidase mutants. Nature 453 (2008) 1258-1261
24. von Itzstein M. Avian influenza virus, a very sticky situation. Curr Opin Chem Biol 12 (2008) 102-108
25. Rich J.R., Gehle D., and von Itzstein M. Design and synthesis of sialidase inhibitors for influenza virus infections. In: Kamerling J.P., Boons G.-J., Lee Y.C., Suzuki A., Taniguchi N., and Voragen A.G.J. (Eds). Comprehensive Glycoscience (2007), Elsevier 885-922
26. ® past, present and future. Future Virol 1 (2006) 577-586
27. Yamada S., Suzuki Y., Suzuki T., Le M.Q., Nidom C.A., Sakai-Tagawa Y., Muramoto Y., Ito M., Kiso M., Horimoto T., et al. Haemagglutinin mutations responsible for the binding of H5N1 influenza A viruses to human-type receptors. Nature 444 (2006) 378-382. The authors describe haemagglutinin mutations that may facilitate the binding of H5N1 influenza virus to human host cell-associated glycans.
28. Stevens J., Blixt O., Tumpey T.M., Taubenberger J.K., Paulson J.C., and Wilson I.A. Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus. Science 312 (2006) 404-410. The authors present an extensive structural and glycan microarray analysis of the haemagglutinin (HA) from H5N1 influenza virus. Linkage specificity and possible determinants for adaptation of an avian influenza virus to successfully infect and transmit human-to-human have been proposed.
29. Nicholls J.M., Chan M.C.W., Chan W.Y., Wong H.K., Cheung C.Y., Kwong D.L.W., Wong M.P., Chui W.H., Poon L.L.M., Tsao S.W., et al. Tropism of avian influenza A (H5N1) in the upper and lower respiratory tract. Nat Med 13 (2007) 147-149. A study on the tropism of the H5N1 avian influenza virus haemagglutinin in the respiratory tract suggesting that haemaggltunin may also be recognising asialoglycan structures.
30. Nicholls J.M., Chan R.W.Y., Russell R.J., Air G.M., and Peiris J.S.M. Evolving complexities of influenza virus and its receptors. Trends Microbiol 16 (2008) 149-157
31. Angulo J., Rademacher C., Biet T., Benie A.J., Blume A., Peters H., Palcic M., Parra F., and Peters T. NMR analysis of carbohydrate-protein interactions. Methods Enzymol 416 (2006) 12-30. An overview of the current NMR methods used to explore carbohydrate-protein interactions.
32. Haselhorst T., Münster-Kühnel A.K., Oschlies M., Tiralongo J., Gerardy-Schahn R., and von Itzstein M. Direct detection of ligand binding to Sepharose-immobilised protein using saturation transfer double difference (STDD) NMR spectroscopy. Biochem Biophys Res Commun 359 (2007) 866-870
33. Haselhorst T., Blanchard H., Frank M., Kraschnefski M.J., Kiefel M.J., Szyczew A.J., Dyason J.C., Fleming F., Holloway G., Coulson B.S., and von Itzstein M. STD NMR spectroscopy and molecular modeling investigation of the binding of N-acetylneuraminic acid derivatives to rhesus rotavirus VP8* core. Glycobiol 17 (2007) 68-81
34. Haselhorst T., Garcia J.-M., Islam T., Lai J.C.C., Rose F.J., Nicholls J.M., Peiris J.S.M., and von Itzstein M. An investigation of avian influenza H5-containing virus-like particles (VLPs) host-cell receptor specificity by STD NMR spectroscopy. Angew Chem Int Ed 47 (2008) 1910-1912
35. Russell R.J., Haire L.F., Stevens D.J., Collins P.J., Lin Y.P., Blackburn G.M., HayAJ, Gamblin S.J., and Skehel J.J. The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design. Nature 443 (2006) 45-49. The first evidence of strain-dependent differences between influenza virus sialidase active sites is provided.
36. Amaro R.E., Minh D.D.L., Cheng L.S., Lindstrom Jr. W.M., Olson A.J., Lin J.-H., Li W.W., and McCammon J.A. Remarkable loop flexibility in avian influenza N1 and its implications for antiviral drug design. J Am Chem Soc 129 (2007) 7764-7765
37. Isa P., Arias C.F., and López S. Role of sialic acids in rotavirus infection. Glycoconj J 23 (2006) 27-37
38. Graham K.L., Sanders N., Tan Y., Allison J., Kay T.W., and Coulson B.S. Rotavirus infection accelerates type 1 diabetes in mice with established insulitis. J Virol 82 (2008) 6139-6149
39. Kraschnefski M.J., Scott S.A., Holloway G., Coulson B.S., von Itzstein M., and Blanchard H. Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the VP8* carbohydrate-binding protein of the human rotavirus strain Wa. Acta Crystallogr Sect F Struct Biol Cryst Commun 61 (2005) 989-993
40. Blanchard H., Yu X., Coulson B.S., and von Itzstein M. Insight into host cell carbohydrate-recognition by human and porcine rotavirus from crystal structures of the virion spike associated carbohydrate-binding domain (VP8*). J Mol Biol 367 (2007) 1215-1226
41. Monnier N., Higo-Moriguchi K., Sun Z.Y., Prasad B.V., Taniguchi K., and Dormitzer P.R. High-resolution molecular and antigen structure of the VP8* core of a sialic acid-independent human rotavirus strain. J Virol 80 (2006) 1513-1523
42. Lamb R.A., and Kolakofsky D. Paramyxoviridae: the viruses and their replication. In: Fields B.N., Knipe D.M., and Howley P.M. (Eds). Fundamental Virology (1996), Lippincott-Raven, Philadelphia 577-604
43. Alymova I.V., Taylor G., Takimoto T., Lin T.H., Chand P., Babu Y.S., Li C., Xiong X., and Portner A. Efficacy of novel hemagglutinin-neuraminidase inhibitors BCX 2798 and BCX 2855 against human parainfluenza viruses in vitro and in vivo. Antimicrob Agents Chemother 48 (2004) 1495-1502
44. Tindal D.J., Dyason J.C., Thomson R.J., Suzuki T., Ueyama H., Kuwahara Y., Maki N., Suzuki Y., and von Itzstein M. Synthesis and evaluation of 4-O-alkylated 2-deoxy-2,3-didehydro-N-acetylneuraminic acid derivatives as inhibitors of human parainfluenza virus type-3 sialidase activity. Bioorg Med Chem Lett 17 (2007) 1655-1658. The authors present a structure-based inhibitor design of compounds that inhibit human parainfluenza 3.
45. Ryan C., Zaitsev V., Tindal D.J., Dyason J.C., Thomson R.J., Alymova I., Portner A., von Itzstein M., and Taylor G. Structural analysis of a designed inhibitor complexed with the hemagglutinin-neuraminidase of Newcastle disease virus. Glycoconj J 23 (2006) 135-141
46. van Poelje P.D., Dang Q., and Erion M.D. Discovery of fructose-1,6-bisphosphatase inhibitors for the treatment of type 2 diabetes. Curr Opin Drug Discov Dev 10 (2007) 430-437
47. Dang Q., Kasibhatla S.R., Reddy K.R., Jiang T., Reddy M.R., Potter S.C., Fujitaki J.M., van Poelje P.D., Huang J., Lipscomb W.N., and Erion M.D. Discovery of potent and specific fructose-1,6-bisphosphatase inhibitors and a series of orally bioavailable phosphoramidase-sensitive prodrugs for the treatment of type 2 diabetes. J Am Chem Soc 129 (2007) 15491-15502
48. Erion M.D., Dang Q., Reddy M.R., Kasibhatla S.R., Huang J., Lipscomb W.N., and van Poelje P.D. Structure-guided design of AMP mimics that inhibit fructose-1,6-bisphosphatase with high affinity and specificity. J Am Chem Soc 129 (2007) 15480-15490
49. Barthel S.R., Gavino J.D., Descheny L., and Dimitroff C.J. Targeting selectins and selectin ligands in inflammation and cancer. Exp Opin Ther Targets 11 (2007) 1473-1491
50. Filser C., Kowalczyk D., Jones C., Wild M.K., Ipe U., Vestweber D., and Kunz H. Synthetic glycopeptides from the E-selectin ligand 1 with varied sialyl Lewis(x) structure as cell-adhesion inhibitors of E-selectin. Angew Chem Int Ed Engl 46 (2007) 2108-2111
51. Kaila N., Janz K., De Bernardo S., Bedard P.W., Camphausen R.T., Tam S., Tsao D.H., Keith Jr. J.C., Nickerson-Nutter C., Shilling A., et al. Synthesis and biological evaluation of quinoline salicylic acids as P-selectin antagonists. J Med Chem 50 (2007) 21-39
52. Kranich R., Busemann A.S., Bock D., Schroeter-Maas S., Beyer D., Heinemann B., Meyer M., Schierhorn K., Zahlten R., Wolff G., and Aydt E.M. Rational design of novel, potent small molecule pan-selectin antagonists. J Med Chem 50 (2007) 1101-1115
53. Ficko-Blean E., Stubbs K.A., Nemirovsky O., Vocadlo D.J., and Boraston A.B. Structural and mechanistic insight into the basis of mucopolysaccharidosis IIIB. Proc Natl Acad Sci U S A 105 (2008) 6560-6565
54. Brumshtein B., Greenblatt H.M., Butters T.D., Shaaltiel Y., Aviezer D., Silman I., Futerman A.H., and Sussman J.L. Crystal structures of complexes of N-butyl and N-nonyl-deoxynojirimycin bound to acid beta-glucosidase: insights into the mechanism of chemical chaperone action in Gaucher disease. J Biol Chem 282 (2007) 29052-29058
55. Park H., Hwang K.Y., Oh K.H., Kim Y.H., Lee J.Y., and Kim K. Discovery of novel alpha-glucosidase inhibitors based on the virtual screening with the homology-modeled protein structure. Bioorg Med Chem 16 (2008) 284-292
56. Crocker P.R., Paulson J.C., and Varki A. Siglecs and their roles in the immune system. Nat Rev Immunol 7 (2007) 255-266
57. Yang RY, Rabinovich GA, Liu FT: Galectins: structure, function and therapeutic potential. Exp Rev Mol Med 2008, in press, doi:10.1017/S146239940800071.
58. Zhuravleva M.A., Trandem K., and Sun P.D. Structural implications of Siglec-5-mediated sialoglycan recognition. J Mol Biol 375 (2008) 437-447
59. Zaccai N.R., May A.P., Robinson R.C., Burtnick L.D., Crocker P.R., Brossmer R., Kelm S., and Jones E.Y. Crystallographic and in silico analysis of the sialoside-binding characteristics of the Siglec sialoadhesin. J Mol Biol 365 (2007) 1469-1479
60. Attrill H., Takazawa H., Witt S., Kelm S., Isecke R., Brossmer R., Ando T., Ishida H., Kiso M., Crocker P.R., and van Aalten D.M. The structure of siglec-7 in complex with sialosides: leads for rational structure-based inhibitor design. Biochem J 397 (2006) 271-278
61. Attrill H., Imamura A., Sharma R.S., Kiso M., Crocker P.R., and van Aalten D.M. Siglec-7 undergoes a major conformational change when complexed with the α(2,8)-disialylganglioside GT1b. J Biol Chem 281 (2006) 32774-32783
62. Maljaars C.E., André S., Halkes K.M., Gabius H.J., and Kamerling J.P. Assessing the inhibitory potency of galectin ligands identified from combinatorial (glyco)peptide libraries using surface plasmon resonance spectroscopy. Anal Biochem 378 (2008) 190-196
63. Oberg C.T., Leffler H., and Nilsson U.J. Arginine binding motifs: design and synthesis of galactose-derived arginine tweezers as galectin-3 inhibitors. J Med Chem 51 (2008) 2297-2301
64. Tejler J., Skogman F., Leffler H., and Nilsson U.J. Synthesis of galactose-mimicking 1H-(1,2,3-triazol-1-yl)-mannosides as selective galectin-3 and 9N inhibitors. Carbohydr Res 342 (2007) 1869-1875
65. Oberg C.T., Blanchard H., Leffler H., and Nilsson U.J. Protein subtype-targeting through ligand epimerization: talose-selectivity of galectin-4 and galectin-8. Bioorg Med Chem Lett 18 (2008) 3691-3694
66. Scott S.A., Scott K., and Blanchard H. Crystallization and preliminary crystallographic analysis of recombinant human galectin-1. Acta Crystallogr Sect F Struct Biol Cryst Commun 63 (2007) 967-971
67. Collins P.M., Hidari K.I., and Blanchard H. Slow diffusion of lactose out of galectin-3 crystals monitored by X-ray crystallography: possible implications for ligand-exchange protocols. Acta Crystallogr D Biol Crystallogr 63 (2007) 415-419
68. Carlsson S., Oberg C.T., Carlsson M.C., Sundin A., Nilsson U.J., Smith D., Cummings R.D., Almkvist J., Karlsson A., and Leffler H. Affinity of galectin-8 and its carbohydrate recognition domains for ligands in solution and at the cell surface. Glycobiology 17 (2007) 663-676
69. Hartshorn M.J. A visualisation aid for structure-based drug design. J Comput Aided Mol Des 16 (2002) 871-881