Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: urinary tract infections (UTI) [ICD11:
GC08 
]
NCBI PubMed ID: 22661447Publication DOI: 10.1093/glycob/cws089Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: wanglei
nankai.edu.cn
Institutions: N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, TEDA School of Biological Sciences and Biotechnology, Tianjin, PR China, Tianjin Key Laboratory of Molecular Nuclear Medicine, Institute of Radiation Medicine, Chinese Academy of Medical Science and Peking Union Medical College, 238 Baidi Road, 300192 Tianjin, P. R. China, Department of Immunobiology of Bacteria, Institute of Microbiology, Biotechnology and Immunology, University of Lodz, PL 90-237 Lodz, Poland
O-Antigen is a component of the outer membrane of Gram-negative bacteria and one of the most variable cell surface constituents, giving rise to major antigenic variability. The diversity of O-antigen is almost entirely attributed to genetic variations in O-antigen gene clusters. Bacteria of the genus Providencia are facultative pathogens, which can cause urinary tract infections, wound infections and enteric diseases. Recently, the O-antigen gene cluster of Providencia was localized between the cpxA and yibK genes in the genome. However, few genes involved in the synthesis of Providencia O-antigens have been functionally identified. In this study, the putative O-antigen gene cluster of Providencia alcalifaciens O30 was sequenced and analyzed. Almost all putative genes for the O-antigen synthesis were found, including a novel formyltransferase gene vioF that was proposed to be responsible for the conversion of dTDP-4-amino-4,6- dideoxy-D-glucose (dTDP-D-Qui4N) to dTDP-4,6-dideoxy-4-formamido-D-glucose (dTDP-D-Qui4NFo). vioF was cloned, and the enzyme product was expressed as a His-tagged fusion protein, purified and assayed for its activity. High-performance liquid chromatography was used to monitor the enzyme-substrate reaction, and the structure of the product dTDP-D-Qui4NFo was established by electrospray ionization tandem mass spectrometry and nuclear magnetic resonance spectroscopy. Kinetic parameters of VioF were determined, and effects of temperature and cations on its activity were also examined. Together, the functional analyses support the identification of the O-antigen gene cluster of P. alcalifaciens O30.
Providencia alcalifaciens, 4, O-antigen gene cluster, formyltransferase, 6-dideoxy-4-formamido-D-glucose biosynthesis
Structure type: monomer
Location inside paper: p.1240, fig.3
Contained glycoepitopes: IEDB_138113,IEDB_196259
Methods: 13C NMR, 1H NMR, NMR-2D, 31P NMR, ESI-MS, genetic methods, biochemical methods, HPLC
Enzymes that release or process the structure: vioF formyltransferase
Biosynthesis and genetic data: genetic data
Related record ID(s): 27232
NCBI Taxonomy refs (TaxIDs): 126385
Show glycosyltransferases
NMR conditions: in D2O at 303(H) K
[as TSV]
13C NMR data:
missing...
1H NMR data:
Linkage Residue H1 H2 H3 H4 H5 H6
5,0,0,4 Fo 8.21
5,0,0 ?DQuip4N 5.58 3.62 3.81 3.72 4.18 1.20
5,0 P
5 P
xXnucdT
1H NMR data:
| Linkage | Residue | H1 | H2 | H3 | H4 | H5 | H6 |
|---|
| 5,0,0,4 | Fo | 8.21 | |
| 5,0,0 | ?DQuip4N | 5.58 | 3.62 | 3.81 | 3.72 | 4.18 | 1.20 |
| 5,0 | P | |
| 5 | P | |
| | xXnucdT | |
|
There is only one chemically distinct structure:
Found 
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