Vi antigen biosynthesis in Salmonella typhi: Characterization of UDP-N-acetylglucosamine C-6 dehydrogenase (TviB) and UDP-N- acetylglucosaminuronic acid C-4 epimerase (TviC)

Biochemistry

Volumn 45, Issue 26, 2006, Pages 8163-8173

  Zhang, Hua ^a   Zhou, Ying ^a   Bao, Hongbo ^a   Liu, Hung Wen ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGENS; BIOSYNTHESIS; CATALYSIS; CLONING; ESCHERICHIA COLI; FUNGI;

ANTIGEN PRODUCTION; N-ACETYLGALACTOSAMINURONATE; SALMONELLA TYPHI; UDP-N-ACETYLGLUCOSAMINE C-6 DEHYDROGENASE (TVIB);

ENZYMES;

BACTERIAL ANTIGEN; DITHIOTHREITOL; EPIMERASE; HISTIDINE; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXIDOREDUCTASE; POLYMER; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE C 6 DEHYDROGENASE; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINURONIC ACID; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINURONIC ACID C 4 EPIMERASE; VI ANTIGEN; VIRULENCE FACTOR;

AMINO ACID SEQUENCE; ARTICLE; BIOSYNTHESIS; BIOTRANSFORMATION; CARBOXY TERMINAL SEQUENCE; CELL FRACTIONATION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME MECHANISM; EPIMERIZATION; ESCHERICHIA COLI; MOLECULAR CLONING; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; SALMONELLA TYPHI;

AMINO ACID SEQUENCE; ANTIGENS, BACTERIAL; BACTERIAL PROTEINS; CARBOHYDRATE DEHYDROGENASES; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CLONING, MOLECULAR; CONSERVED SEQUENCE; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR SEQUENCE DATA; POLYSACCHARIDES, BACTERIAL; PSEUDOMONAS AERUGINOSA; RECOMBINANT PROTEINS; SALMONELLA TYPHI; SEQUENCE ALIGNMENT; VIRULENCE;

ESCHERICHIA COLI; SALMONELLA TYPHI;

EID: 33745612125     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060446d     Document Type: Article

References (30)

1. Baker, E. E., Whiteside, R. E., Basch, R., and Derow, M. A. (1959) The Vi antigen of the Enterobacteriaceae. II. Immunologic and biologic properties, J. Immunol. 83, 680-686.
2. Su, S. C., and Bystrichy, S. (2003) Physical, chemical, antigenic, and immunologie characterization of polygalacturonan, its derivatives, and Vi antigen from Salmonella typhi, Methods Enzymol. 363, 552-567.
3. Virloguex-Payant, I., and Popoff, M. Y. (1996) The Vi antigen of Salmonella typhi, Bull. Inst. Pasteur 94, 237-250.
4. Felix, A., and Pitt, R. (1934) Virulence of B. typhosus and resistance to O antibody, J. Pathol. Bacteriol. 38, 409-420.
5. Klugman, K. P., Koornhof, H. J., Robbins, J. B., and Le Cam, N. N. (1996) Immunogenicity, efficacy and serological correlate of protection of Salmonella typhi Vi capsular polysaccharide vaccine three years after immunization, Vaccine 14, 435-438.
6. Johnson, E. M., and Baron, L. S. (1969) Genetic transfer of the Vi antigen from Salmonella typhosa to Escherichia coli, J. Bacterial. 99, 355-359.
7. Pickard, D., Li, J., Roberts, M., Maskell, D., Hone, D., Levine, M., Dougan, G., and Chatfield, S. (1994) Characterization of defined ompR mutants of Salmonella typhi: ompR is involved in the regulation of Vi polysaccharide expression, Infect. Immun. 62, 3984-3993.
8. Johnson, E. M., Krauskopf, B., and Baron, L. S. (1965) Genetic mapping of Vi and somatic antigenic determinants in Salmonella, J. Bacterial. 90, 302-308.
9. Hashimoto, Y., Li, N., Yokoyama, H., and Ezaki, T. (1993) Complete nucleotide sequence and molecular characterization of viaB region encoding Vi antigen in Salmonella typhi, J. Bacteriol. 175, 4456-4465.
10. Waxin, H., Virlogeux, I., Kolyva, S., and Popoff, M. Y. (1993) Identification of six open reading fames in the Salmonella enterica subsp. Enterica ser, Typhi viaB locus involved in Vi antigen production, Res. Microbiol. 144, 363-371.
11. Virlogeux, I., Waxin, H., Ecobichon, C., and Popoff, M. Y. (1995) Role of the viaB locus in synthesis, transport and expression of Salmonella typhi Vi antigen, Microbiology 141, 3039-3047.
12. Campbell, R. E., Sala, R. R, van de Rijn, I., and Tanner, M. E. (1997) Properties and kinetic analysis of UDP-glucose dehydrogenase from group A Streptococci, J. Biol. Chem. 272, 3416-3422.
13. Campbell, R. E., Mosimann, S. C., Rijin, I., Tanner, M. E., and Strynadka, N. C. J. (2000) The first structure of UDP-glucose dehydrogenase reveals the catalytic residues necessary for the two-fold oxidation, Biochemistry 39, 7012-7023.
14. Ge, X., Penney, L. C., van de Rijn, I., and Tanner, M. E. (2004) Active site residues and mechanism of UDP-glucose dehydrogenase, Eur. J. Biochem. 271, 14-22.
15. Zhao, X., Creuzenet, C., Belanger, M., Egbosimba, E., Li, J., and Lam, J. S. (2000) WbpO, a UDP-N-acetyl-D-galactosamine dehydrogenase from Pseudomonas aeruginosa Serotype O6, J. Biol. Chem. 275, 33252-33259.
16. Miller, W. L., Wenzel, C. Q, Daniels, C., Larocque, S., Brisson, J., and Lam, J. S. (2004) Biochemical characterization of WbpA, a UDP-N-acetyl-D- glucosamine 6-dehydrogenase involved in O-antigen biosynthesis in Pseudomonas aeruginosa PAO1, J. Biol. Chem. 279, 37551-37558.
17. Reid, M. F., and Fewson, C. A. (1994) Molecular characterization of microbial alcohol dehydrogenases, Crit. Rev. Microbiol. 20, 13-56.
18. Kowal, P., and Wang, P. G. (2002) New UDP-GlcNAc C4 epimerase involved in the biosynthesis of 2-acetamino-2-deoxy-L-altruronic acid in the O-antigen repeating units of Plesiomonas shigelloides O17, Biochemistry 41, 15410-15414.
19. Creuzenet, C., Belanger, M., Wakarchuk, W. W., and Lam, J. S. (2000) Expression, purification and biochemical characterization of WbpP, a new UDP-GlcNAc C4 epimerase from Pseudomonas aeruginosa Serotype O6, J. Biol. Chem. 275, 19060-19067.
20. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
21. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual, 2nd ed., Cold Spring Harbor, Cold Spring Harbor, NY.
22. Andrews, P. (1964) Estimation of the molecular weights of proteins by sephadex gel-filtration, Biochem. J. 91, 222-233.
23. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
24. The QIAexpressionist, A Handbook for High-Level Expression and Purification of 6x His-Tagged Proteins, 5th ed., March 2001, pp 72-75, QIAGEN.
25. Thoden, J. B., Frey, P. A., and Holden, H. M. (1996) Crystal structures of the oxidized and reduced forms of UDP-galactose 4-epimerase isolated from Escherichia coli, Biochemistry 35, 2557-2566.
26. Thoden, J. B., Frey, P. A., and Holden, H. M. (1996) Molecular structure of the NADH/UDP-glucose abortive complex of UDP-galactose 4-epimerase from Escherichia coli: implications for the catalytic mechanism, Biochemistry 35, 5137-5144.
27. Thoden, J. B., Wohlers, T. M., Fridovich-Keil, J. L., and Holden, H. M. (2001) Human UDP-galactose 4-epimerase. Accommodation of UDP-N-acetylglucosamine within the active site, J. Biol. Chem. 276, 15131-15136.
28. Schulz, J. M., Watson, A. L., Sanders, R., Ross, K. L., Thoden, J. B., Holden, H. M., and Fridovich-Keil, J. L. (2004) Determinants of function and substrate specificity in human UDP-galactose 4′-epimerase, J. Biol. Chem. 279, 32796-32803.
29. Demendi, M., Ishiyama, N., Lam, J. S., Berghuis, A. M., and Creuzenet, C. (2005) Towards a better understanding of the substrate specificity of the UDP-N-acetylglucosamine C4 epimerase WbpP, Biochem J. 389, 173-180.
30. Belanger, M., Burrows, L. L., and Lam, J. S. (1999) Functional analysis of genes responsible for the synthesis of the B-band O antigen of Pseudomonas aeruginosa serotype O6 lipopolysaccharide, Microbiology 145, 3505-3521.