Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Host organism: Homo sapiens
Associated disease: urinary tract infections (UTI) [ICD11:
GC08 
];
infection due to Proteus mirabilis [ICD11:
XN9ZF ];
infection due to Klebsiella pneumoniae [ICD11:
XN741 ]
NCBI PubMed ID: 20959463Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: jtomas
ub.edu
Institutions: Departamento de Microbiologia y Parasitologia Sanitarias, Facultad de Farmacia, Universidad de Barcelona, 08028 Barcelona, Spain
The core lipopolysaccharides (LPS) of Proteus mirabilis as well as those of Klebsiella pneumoniae and Serratia marcescens are characterized by the presence of a hexosamine-galacturonic acid disaccharide (αHexN-(1,4)-αGalA) attached by an α1,3 linkage to L-glycero-D-manno-heptopyranose II (L-glycero-α-D-manno-heptosepyranose II). In K. pneumoniae, S. marcescens, and some P. mirabilis strains, HexN is D-glucosamine, whereas in other P. mirabilis strains, it corresponds to D-galactosamine. Previously, we have shown that two enzymes are required for the incorporation of D-glucosamine into the core LPS of K. pneumoniae; the WabH enzyme catalyzes the incorporation of GlcNAc from UDP-GlcNAc to outer core LPS, and WabN catalyzes the deacetylation of the incorporated GlcNAc. Here we report the presence of two different HexNAc transferases depending on the nature of the HexN in P. mirabilis core LPS. In vivo and in vitro assays using LPS truncated at the level of galacturonic acid as acceptor show that these two enzymes differ in their specificity for the transfer of GlcNAc or GalNAc. By contrast, only one WabN homologue was found in the studied P. mirabilis strains. Similar assays suggest that the P. mirabilis WabN homologue is able to deacetylate both GlcNAc and GalNAc. We conclude that incorporation of d-galactosamine requires three enzymes: Gne epimerase for the generation of UDP-GalNAc from UDP-GlcNAc, N-acetylgalactosaminyltransferase (WabP), and LPS:HexNAc deacetylase.
Lipopolysaccharide, core, Proteus mirabilis, Serratia marcescens, epimerase, Klebsiella pneumoniae, transferases
Structure type: oligomer
Location inside paper: p.39743, fig.1A
Aglycon: lipid A
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130650,IEDB_130659,IEDB_130670,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_142488,IEDB_146664,IEDB_2189047,IEDB_226811,IEDB_983931,SB_192
Methods: PCR, GC-MS, SDS-PAGE, MALDI-TOF MS, genetic methods, biochemical methods, SDS-Tricine-PAGE
Enzymes that release or process the structure: wabH,wabP,wabN
Biosynthesis and genetic data: genetic data, biochemical data
Comments, role: The common part of core OS shared by all the studied strains of P. mirabilis, K. pneumoniae, and S. marcescens.
Related record ID(s): 25505, 25506
NCBI Taxonomy refs (TaxIDs): 584,
573,
615
Show glycosyltransferases
There is only one chemically distinct structure:
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