Molecular and genetic analyses of the putative Proteus O antigen gene locus

Applied and Environmental Microbiology

Volumn 76, Issue 16, 2010, Pages 5471-5478

  Wang, Quan ^a,b   Torzewska, Agnieszka ^c   Ruan, Xiaojuan ^a,b   Wang, Xiaoting ^a,b   Rozalski, Antoni ^c   Shao, Zhujun ^d   Guo, Xi ^a,b   Zhou, Haijian ^d   Feng, Lu ^a,e,f   Wang, Lei ^a,b,e,f  

^a NANKAI UNIVERSITY   (China)

^b BEIJING UNIVERSITY OF POSTS AND TELECOMMUNICATIONS   (China)

^c UNIVERSITY OF LODZ   (Poland)

^d CHINESE CENTER FOR DISEASE CONTROL AND PREVENTION   (China)

^e Tianjin Key Laboratory of Microbial Functional Genomics   (China)

^f Tianjin Research Center for Functional Genomics and Biochip   (China)

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACES; DEGREE OF HETEROGENEITIES; GENETIC ANALYSIS; MOLECULAR CHARACTERIZATION; MOLECULAR CLASSIFICATION; O-ANTIGEN; O-ANTIGEN GENE CLUSTER; O-ANTIGEN GENES; PROTEUS SPECIES; RESTRICTION FRAGMENT LENGTH POLYMORPHISMS; SEROGROUPS; URINARY TRACT INFECTIONS;

CELL MEMBRANES; GENES;

ANTIGENS;

BACTERIAL DNA; O ANTIGEN;

BACTERIUM; DATABASE; GENE EXPRESSION; GENETIC ANALYSIS; HETEROGENEITY; MOLECULAR ANALYSIS; PATHOGEN; POLYMERASE CHAIN REACTION; POLYMORPHISM;

ARTICLE; BACTERIAL GENE; CHEMISTRY; CLUSTER ANALYSIS; DNA FINGERPRINTING; DNA SEQUENCE; GENETIC POLYMORPHISM; GENETICS; HUMAN; MOLECULAR GENETICS; MULTIGENE FAMILY; NUCLEOTIDE SEQUENCE; PHYLOGENY; PROTEUS; RESTRICTION FRAGMENT LENGTH POLYMORPHISM; SEQUENCE HOMOLOGY;

CLUSTER ANALYSIS; DNA FINGERPRINTING; DNA, BACTERIAL; GENES, BACTERIAL; HUMANS; MOLECULAR SEQUENCE DATA; MULTIGENE FAMILY; O ANTIGENS; PHYLOGENY; POLYMORPHISM, GENETIC; POLYMORPHISM, RESTRICTION FRAGMENT LENGTH; PROTEUS; SEQUENCE ANALYSIS, DNA; SEQUENCE HOMOLOGY;

EID: 77955939182     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.02946-09     Document Type: Article

References (42)

1. Alamuri, P., andH. L. Mobley. 2008. A novel autotransporter of uropathogenic Proteus mirabilis is both a cytotoxin and an agglutinin. Mol. Microbiol. 68:997-1017.
2. Alexander, D. C., andM. A. Valvano. 1994. Role of the rfe gene in the biosynthesis of the Escherichia coli 07-specific lipopolysaccharide and other O-specific polysaccharides containing N-acetylglucosamine. J. Bacteriol. 176: 7079-7084.
3. Bastin, D. A., andP. R. Reeves. 1995. Sequence and analysis of the O antigen gene (rfb) cluster of Escherichia coli O111. Gene 164:17-23.
4. Bateman, A., E. Birney, L. Cerruti, R. Durbin, L. Etwiller, S. R. Eddy, S. Griffiths-Jones, K. L. Howe, M. Marshall, andE. L. Sonnhammer. 2002. The Pfam protein families database. Nucleic Acids Res. 30:276-280.
5. Bengoechea, J. A., E. Pinta, T. Salminen, C. Oertelt, O. Holst, J. Radziejewska-Lebrecht, Z. Piotrowska-Seget, R. Venho, andM. Skurnik. 2002. Functional characterization of Gne (UDP-N-acetylglucosamine-4-epimerase), Wzz (chain length determinant), and Wzy (O-antigen polymerase) of Yersinia enterocolitica serotype 0:8. J. Bacteriol. 184:4277-4287.
6. Beutin, L., Q. Wang, D. Naumann, W. Han, G. Krause, L. Leomil, L. Wang, andL. Feng. 2007. Relationship between O-antigen subtypes, bacterial surface structures and O-antigen gene clusters in Escherichia coli 0123 strains carrying genes for Shiga toxins and intimin. J. Med. Microbiol. 56:177-184.
7. Beynon, L. M., A. J. Dumanski, R J. McLean, L. L. MacLean, J. C. Richards, andM. B. Perry. 1992. Capsule structure of Proteus mirabilis (ATCC 49565). J. Bacteriol. 174:2172-2177.
8. Daniels, C., C. Vindurampulle, andR. Morona. 1998. Overexpression and topology of the Shigella flexneri O-antigen polymerase (Rfc/Wzy). Mol. Microbiol. 28:1211-1222.
9. Feng, L., W. Han, Q. Wang, D. A. Bastin, andL. Wang. 2005. Characterization of Escherichia coli 086 O-antigen gene cluster and identification of 086-specific genes. Vet. Microbiol. 106:241-248.
10. Fritz, K. 1966. The bacteriology of Enterobacteriaceae. Williams & Wilkins, Baltimore, Md.
11. Jacobsen, S. M., M. C. Lane, J. M. Harro, M. E. Shirtliff, andH. L. Mobley. 2008. The high-affinity phosphate transporter Pst is a virulence factor for Proteus mirabilis during complicated urinary tract infection. FEMS Immunol. Med. Microbiol. 52:180-193.
12. Jacobsen, S. M., D. J. Stickler, H. L. Mobley, andM. E. Shirtliff. 2008. Complicated catheter-associated urinary tract infections due to Escherichia coli and Proteus mirabilis. Clin. Microbiol. Rev. 21:26-59.
13. Kaca, W., M. Arabski, R. Fudala, E. Holmstrom, A. Sjoholm, A. Weintraub, B. Futoma-Koloch, G. Bugla-Ploskonska, andW. Doroszkiewicz. 2009. Human complement activation by smooth and rough Proteus mirabilis lipopolysaccharides. Arch. Immunol. Ther. Exp. 57:383-391.
14. Kaca, W., I. A. Knirel, E. V. Vinogradov, andK. Kotelko. 1987. Structure of the O-specific polysaccharide of Proteus mirabilis S1959. Arch. Immunol. Ther. Exp. (Warsz.) 35:431-437.
15. Kim, B. N., N. J. Kim, M. N. Kim, Y. S. Kim, J. H. Woo, andJ. Ryu. 2003. Bacteraemia due to tribe Proteeae: a review of 132 cases during a decade (1991-2000). Scand. J. Infect. Dis. 35:98-103.
16. Knirel, Y. A., W. Kaca, A. Rozalski, andZ. Sidorczyk. 1990. Structure of O-antigenic polysaccharides of Proteus bacilli. Pol. J. Chem. 73:859-907.
17. Liu, D., R. A. Cole, andP. R. Reeves. 1996. An O-antigen processing function for Wzx(RfbX): a promising candidate for O-unit flippase. J. Bacteriol. 178:2102-2107.
18. Mobley, H. L., andR. Belas. 1995. Swarming and pathogenicity of Proteus mirabilis in the urinary tract. Trends Microbiol. 3:280-284.
19. Nassau, P. M., S. L. Martin, R. E. Brown, A. Weston, D. Monsey, M. R. McNeil, andK. Duncan. 1996. Galactofuranose biosynthesis in Escherichia coli K-12: identification and cloning of UDF-galactopyranose mutase. J. Bacteriol. 178:1047-1052.
20. O'Hara, C. M., F. W. Brenner, andJ. M. Miller. 2000. Classification, identification, and clinical significance of Proteus, Providencia, and Morganella. Clin. Microbiol. Rev. 13:534-546.
21. O'Hara, C. M., F. W. Brenner, A. G. Steigerwalt, B. C. Hill, B. Holmes, P. A. Grimont, P. M. Hawkey, J. L. Penner, J. M. Miller, andD. J. Brenner. 2000. Classification of Proteus vulgaris biogroup 3 with recognition of Proteus hauseri sp. nov., nom. rev. and unnamed Proteus genomospecies 4, 5 and 6. Int. J. Syst. Evol. Microbiol. 50:1869-1875.
22. Pearson, M. M., M. Sebaihia, C. Churcher, M. A. Quail, A. S. Seshasayee, N. M. Luscombe, Z. Abdellah, C. Arrosmith, B. Atkin, T. Chillingworth, H. Hauser, K. Jagels, S. Moule, K. Mungall, H. Norbertczak, E. Rabbinowitsch, D. Walker, S. Whithead, N. R. Thomson, P. N. Rather, J. Parkhill, and H. L. Mobley. 2008. Complete genome sequence of uropathogenic Proteus mirabilis, a master of both adherence and motility. J. Bacteriol. 190:4027-4037.
23. Penner, J. L., andJ. N. Hennessy. 1980. Separate O-grouping schemes for serotyping clinical isolates of Proteus vulgaris and Proteus mirabilis. J. Clin. Microbiol. 12:304-309.
24. Perepelov, A. V., A. S. Shashkov, D. Babichka, S. N. Senchenkova, B. Bartodziejska, A. Rozalski, andY. A. Knirel. 2000. Structure of the O-specific polysaccharide of the bacterium Proteus vulgaris 023. Biochemistiy (Mosc.) 65:1055-1059.
25. Perry, M. B., andL. L. MacLean. 1994. The structure of the polysaccharide produced by Proteus vulgaris (ATCC 49990). Carbohydr. Res. 253:257-263.
26. Raetz, C. R., andC. Whitfield. 2002. Lipopolysaccharide endotoxins. Annu. Rev. Biochem. 71:635-700.
27. Rozalski, A. 2008. Lipopolysaccharide (LPS, endotoxin) of Proteus bacteria-chemical structure, serological specificity and the role in the pathogenicity. Folia Biol. Oecol. 4:5-24.
28. Rozalski, A., Z. Sidorczyk, andK. Kotelko. 1997. Potential virulence factors of Proteus bacilli. Microbiol. Mol. Biol. Rev. 61:65-89.
29. Rozalski, A., A. Torzewska, B. Bartodziejska, D. Babichka, I. Kwil, A. V. Perepelov, A. N. Kondakova, S. N. Senchenkova, I. A. Knirel, andE. V. Vinogradov. 2002. Chemical structure, antigenic specificity and the role in the pathogenicity of lipopolysaccharide (LPS, endotoxin) on Proteus vulgaris bacteria's example. Wiad. Chem. 56:585-604.
30. Rutherford, K., J. Parkhill, J. Crook, T. Horsnell, P. Rice, M. A. Rajandream, andB. Barrell. 2000. Artemis: sequence visualisation and annotation. Bioinformatics 16:944-945.
31. Staden, R. 1996. The Staden sequence analysis package. Mol. Biotechnol. 5:233-241.
32. St. Swierzko, A., A. S. Shashkov, S. N. Senchenkova, F. V. Toukach, A. Ziolkowski, M. Cedzynski, N. A. Paramonov, W. Kaca, andY. A. Knirel. 1996. Structural and serological studies of the O-specific polysaccharide of the bacterium Proteus mirabilis O10 containing L-altruronic acid, a new component of O-antigens. FEBS Lett. 398:297-302.
33. Tatusov, R L., D. A. Natale, I. V. Garkavtsev, T. A. Tatusova, U. T. Shankavaram, B. S. Rao, B. Kiryutin, M. Y. Galperin, N. D. Fedorova, andE. V. Koonin. 2001. The COG database: new developments in phylogenetic classification of proteins from complete genomes. Nucleic Acids Res. 29:22-28.
34. Thompson, J. D., D. G. Higgins, andT. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
35. Torzewska, A., P. Staczek, andA. Rozalski. 2003. Crystallization of urine mineral components may depend on the chemical nature of Proteus endotoxin polysaccharides. J. Med. Microbiol. 52:471-477.
36. Usadel, B., U. Schluter, M. Molhoj, M. Gipmans, R. Verma, J. Kossmann, W. D. Reiter, andM. Pauly. 2004. Identification and characterization of a UDP-D-glucuronate 4-epimerase in Arabidopsis. FEBS Lett. 569:327-331.
37. Vigetti, D., M. Ori, M. Viola, A. Genasetti, E. Karousou, M. Rizzi, F. Pallotti, I. Nardi, V. C. Hascall, G. De Luca, and A. Passi. 2006. Molecular cloning and characterization of UDP-glucose dehydrogenase from the amphibian Xenopus laevis and its involvement in hyaluronan synthesis. J. Biol. Chem. 281:8254-8263.
38. Vinogradov, E. V., D. Krajewska-Pietrasik, W. Kaca, A. S. Shashkov, Y. A. Knirel, andN. K. Kochetkov. 1989. Structure of Proteus mirabilis 027 O-specific polysaccharide containing amino acids and phosphoethanolamine. Eur. J. Biochem. 185:645-650.
39. Wang, L., S. Huskic, A. Cisterne, D. Rothemund, andP. R. Reeves. 2002. The O-antigen gene cluster of Escherichia coli O55:H7 and identification of a new UDP-GlcNAc C4 epimerase gene. J. Bacteriol. 184:2620-2625.
40. Wang, L., andP. R. Reeves. 1994. Involvement of the galactosyl- 1-phosphate transferase encoded by the Salmonella enterica rfbP gene in O-antigen subunit processing. J. Bacteriol. 176:4348-4356.
41. Wang, L., andP. R. Reeves. 1998. Organization of Escherichia coli 0157 O antigen gene cluster and identification of its specific genes. Infect. Immun. 66:3545-3551.
42. Zych, K., M. Kowalczyk, Y. A. Knirel, andZ. Sidorczyk. 2000. New serogroups of the genus Proteus consisting of Proteus penneri strains only. Determination of some LPS epitopes responsible for specificity. Adv. Exp. Med. Biol. 485:339-344.