Carboxyl terminus of Helicobacter pylori α1,3-fucosyltransferase determines the structure and stability

Biochemistry

Volumn 45, Issue 26, 2006, Pages 8108-8116

  Lin, Sheng Wei ^a,b   Yuan, Tsui Min ^a,b   Li, Jei Ru ^a   Lin, Chun Hung ^a,b  

^a INSTITUTE OF BIOLOGICAL CHEMISTRY   (Taiwan)

^b NATIONAL TAIWAN UNIVERSITY   (Taiwan)

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; ANTIGENS; BACTERIA; CARBOHYDRATES; HYDROPHOBICITY; IMMUNOLOGY; POLYSACCHARIDES; SPECTROSCOPY; STRUCTURAL ANALYSIS;

CARBOHYDRATE ANTIGENS; ENZYMATIC ACTIVITY; HELICOBACTER PYLORI; IMMUNE SYSTEM;

ENZYMES;

ACETIC ACID DERIVATIVE; ALPHA 1,3 FUCOSYLTRANSFERASE; CARBOHYDRATE ANTIGEN; DIMER; EPITOPE; FUCOSE; GUANOSINE DIPHOSPHATE FUCOSE; LIPOPOLYSACCHARIDE; N ACETYLLACTOSAMINE; O ANTIGEN; UNCLASSIFIED DRUG;

ANALYTIC METHOD; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; DUODENUM ULCER; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME MECHANISM; ENZYME STABILITY; ENZYME STRUCTURE; GASTRITIS; HELICOBACTER PYLORI; HIGH TEMPERATURE; HOST; HYDROPHOBICITY; IMMUNE SYSTEM; NONHUMAN; PRIORITY JOURNAL; SOLUBILITY; STOMACH CANCER; STOMACH EPITHELIUM; TANDEM REPEAT; ULTRACENTRIFUGATION;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BASE SEQUENCE; CIRCULAR DICHROISM; DNA PRIMERS; ENZYME STABILITY; FUCOSYLTRANSFERASES; HELICOBACTER PYLORI; KINETICS; MOLECULAR SEQUENCE DATA; POLYMERASE CHAIN REACTION; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; ULTRACENTRIFUGATION;

HELICOBACTER PYLORI;

EID: 33745606217     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0601297     Document Type: Article

References (39)

1. Dubois, A. (1995) Spiral bacteria in the human stomach: the gastric helicobacters, Emerging Infect. Dis. 1, 79-85.
2. Peterson, W. I. (1991) Helicobacter pylori and peptic ulcer disease, N. Engl. J. Med. 324, 1043-1048.
3. Parsonnet, J. (1996) Helicobacter pylori in the stomach-a paradox unmasked, N. Engl. J. Med. 335, 278-280.
4. Nakamura, S., Yao, T., Aoyagi, K., Iida, M., Fujishima, M., and Tsuneyoshi, M. (1997) Helicobacter pylori and primary gastric lymphoma. A histopathologic and immunohistochemical analysis of 237 patients, Cancer 79, 3-11.
5. Ilver, D., Arnqvist, A., Ogren, J., Frick, I. M., Kersulyte, D., Incecik, E. T., Berg, D. E., Covacci, A., Engstrand, L., and Boren, T. (1998) Helicobacter pylori adhesin binding fucosylated histoblood group antigens revealed by retagging, Science 279, 373-377.
6. Guruge, J. L., Falk, P. G., Lorenz, R. G., Dans, M., Wirth, H. P., Blaser, M. J., Berg, D. E., and Gordon, J. I. (1998) Epithelial attachment alters the outcome of Helicobacter pylori infection, Proc. Natl. Acad. Sci. U.S.A. 95, 3925-3930.
7. Mahdavi, J., Sonden, B., Hurtig, M., Olfat, F. O., Forsberg, L., Roche, N., Angstrom, J., Larsson, T., Teneberg, S., Karlsson, K. A., Altraja, S., Wadstrom, T., Kersulyte, D., Berg, D. E., Dubois, A., Petersson, C., Magnusson, K. E., Norberg, T., Lindh, F., Lundskog, B. B., Arnqvist, A., Hammarstrom, L., and Boren, T. (2002) Helicobacter pylori SabA adhesin in persistent infection and chronic inflammation, Science 297, 573-578.
8. Linden, S., Boren, T., Dubois, A., and Carlstedt, I. (2004) Rhesus monkey gastric mucins: oligomeric structure, glycoforms and Helicobacter pylori binding, Biochem. J. 379, 765-775.
9. Kannagi, R., Izawa, M., Koike, T., Miyazaki, K., and Kimura, N. (2004) Carbohydrate-mediated cell adhesion in cancer metastasis and angiogenesis, Cancer Sci. 95, 377-384.
10. Dube, D. H., and Bertozzi, C. R. (2005) Glycans in cancer and inflammation-potential for therapeutics and diagnostics, Nat. Rev. Drug Discovery 4, 477-488.
11. Hynes, S. O., Keenan, J. I., Ferris, J. A., Annuk, H., and Moran, A. P. (2005) Lewis epitopes on outer membrane vesicles of relevance to Helicobacter pylori pathogenesis, Helicobacter 10, 146-156.
12. Moran, A. P., Prendergast, M. M., and Appelmelk, B. J. (1996) Molecular mimicry of host structures by bacterial lipopolysaccharides and its contribution to disease, FEMS Immunol. Med. Microbiol. 161, 105-115.
13. Lozniewski, A., Haristoy, X., Rasko, D. A., Hatier, R., Plénat, F., Taylor, D. E., and Angioi-Duprez, K. (2003) Influence of Lewis antigen expression by Helicobacter pylori on bacterial internalization by gastric epithelial cells, Infect. Immun. 71, 2902-2906.
14. Teixeira, A., David, L., Reis, C. A., Costa, J., and Sobrinho-Simoes, M. (2002) Expression of mucins (MUC1, MUC2, MUC5AC, and MUC6) and type 1 Lewis antigens in cases with and without Helicobacter pylori colonization in metaplastic glands of the human stomach, J. Pathol. 197, 37-43.
15. Backstrom, A., Lundberg, C., Kersulyte, D., Berg, D. E., Boren, T., and Arnqvist, A. (2004) Metastability of Helicobacter pylori bab adhesin genes and dynamics in Lewis b antigen binding, Proc. Natl. Acad. Sci. U.S.A. 101, 16923-16928.
16. Moran, A. P., Knirel, Y. A., Senchenkova, S. N., Widmalm, G., Hynes, S. O., and Jansson, P. E. (2002) Phenotypic variation in molecular mimicry between Helicobacter pylori lipopolysaccharides and human gastric epithelial cell surface glycoforms. Acid-induced phase variation in Lewis(x) and Lewis(y) expression by H. Pylori lipopolysaccharides, J. Biol. Chem. 277, 5785-5795.
17. Wang, G., Ge, Z., Rasko, D. A., and Taylor, D. E. (2000) Lewis antigens in Helicobacter pylori: biosynthesis and phase variation, Mol. Microbiol. 36, 1187-1196.
18. Kleene, R., and Berger, E. G. (1993) The molecular and cell biology of glycosyltransferases, Biochim. Biophys. Acta 1154, 283-325.
19. Ge, Z., Chan, N. W., Palcic, M. M., and Taylor, D. E. (1997) Cloning and heterologous expression of an alpha1,3-fucosyltransferase gene from the gastric pathogen Helicobacter pylori, J. Biol. Chem. 272, 21357-21363.
20. Wakarchuk, W. W., Cunningham, A., Watson, D. C., and Young, N. M., (1998) Role of paired basic residues in the expressioa of active recombinant galactosyltransferases from the bacterial pathogen Neisseria meningitidis, Protein Eng. 11, 295-302.
21. Lin, S. W., Wu, I. L., and Lin, C. H. (2005) Substrate specificity study of α1,3-fucosyltransferase from Helicobacter pylori. Glycoconjugate J. 22, 186. The preliminary result was also reported at the Glyco XVIII International Symposium on Glycoconjugates in September 4-9, 2005 in Florence, Italy.
22. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989). Molecular Cloning- A Laboratory Manual, 2nd ed, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
23. Murray, B. W., Wittmann, V., Burkart, M. D., Hung, S. C., and Wong, C. H. (1997) Mechanism of human α1,3-fucosyltransferase V: Glycosidic cleavage occurs prior to nucleophilic attack, Biochemistry 36, 823-831.
24. Ma, B., Wang, G., Palcic, M. M., Hazes, B., and Taylor, D. E. (2003) C-terminal amino acids of Helicobacter pylori alpha1,3/4 fucosyltransferases determine type I and type II transfer, J. Biol. Chem. 278, 21893-21900.
25. Martin, S. L., Edbrooke, M. R., Hodgman, T. C., van den Eijnden, D. H., and Bird, M. I. (1997) Lewis X biosynthesis in Helicobacter pylori: Molecular cloning of an (1,3)-fucosyltransferase gene, J. Biol. Chem. 272, 21349-21356.
26. Sreerama, N., and Woody, R. W. (2004) Computation and analysis of protein circular dichroism spectra, Methods Enzymol. 383, 318-351.
27. Sreerama, N., and Woody, R. W. (2000) Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set, Anal. Biochem. 287, 252-260.
28. Sreerama, N., Venyaminov, S. Y., and Woody, R. W. (2000) Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis, Anal. Biochem. 287, 243-251.
29. Pace, C. N. (1986) Determination and analysis of urea and guanidine hydrochloride denaturation curves, Methods Enzymol. 131, 266-280.
30. Rasko, D. A., Wang, G., Palcic, M. M., and Taylor, D. E. (2000) Cloning and characterization of the alpha(1,3/4) fucosyltransferase of Helicobacter pylori, J. Biol. Chem. 275, 4988-4994.
31. Ma, B., Lau, L. H., Palcic, M. M., Hazes, B., and Taylor, D. E. (2005) A single aromatic amino acid at the carboxyl terminus of Helicobacter pylori alpha-1,3/4 fucosyltransferase determines substrate specificity, J. Biol. Chem. 280, 36848-36856.
32. de Vries, T., Knegtel, R. M., Holmes, E. H., and Macher, B. A. (2001) Fucosyltransferases: structure/function studies, Glycobiology 11, 119R-128R.
33. Oriol, R., Mollicone, R., Cailleau, A., Balanzino, L., and Breton, C. (1999) Divergent evolution of fucosyltransferase genes from vertebrates, invertebrates, and bacteria, Glycobiology 9, 323-34.
34. Opat, A. S., Houghton, F., and Gleeson, P. A. (2000) Medial Golgi but not late Golgi glycosyltransferases exist as high molecular weight complexes. Role of luminal domain in complex formation and localization, J. Biol. Chem. 275, 11836-11845.
35. Fenteany, F. H., and Colley, K. J. (2005) Multiple signals are required for alpha2,6-sialyltransferase (ST6Gal I) oligomerization and Golgi localization, J. Biol. Chem. 280, 5423-5429.
36. El-Battari, A., Prorok, M., Angata, K., Mathieu, S., Zerfaoui, M., Ong, E., Suzuki, M., Lombardo, D., and Fukuda, M. (2003) Different glycosyltransferases are differentially processed for secretion, dimerization, and autoglycosylation, Glycobiology 13, 941-953.
37. Qian, R., Chen, C., and Colley, K. J. (2001) Location and mechanism of alpha 2,6-sialyltransferase dimer formation. Role of cysteine residues in enzyme dimerization, localization, activity, and processing, J. Biol. Chem. 276, 28641-28649.
38. Appelmelk, B. J., Shiberu, B., Trinks, C., Tapsi, N., Zherig, P. Y., Verboom, T., Maaskant, J., Hokke, C. H., Schiphors, W. E., Blanchard, D., Simoons-Smit, I. M, van den Eijnden, D. H., and Vandenbroucke-Grauls, C. M. (1998) Phase variation in Helicobacter pylori lipopolysaccharide, Infect. Immun. 66, 70-76.
39. Appelmelk, B. J., Martin, S. L., Monteiro, M. A., Clayton, C. A., McColm, A. A., Zheng, P., Verboom, T., Maaskant, J. J., van den Eijnden, D. H., Hokke, C. H., Perry, M. B., Vandenbroucke-Grauls, C. M., and Kusters, J. G. (1999) Phase variation in Helicobacter pylori lipopolysaccharide due to changes in the lengths of poly(C) tracts in alpha3-fucosyltransferase genes, Infect. Immun. 67, 5361-5366.