Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Yersinia enterocolitica [ICD11:
XN91V 
]
NCBI PubMed ID: 9048864Publication DOI: 10.1111/j.1699-0463.1996.tb04951.xJournal NLM ID: 8803400Publisher: Copenhagen: Munksgaard
Institutions: Turku Centre for Biotechnology, University of Turku, Finland, department of Medical Microbiology, University of Turku, Turku, Finland
Studies on the molecular genetics of bacterial LPS serve at least two main purposes: (i) to help develop an understanding of the biology, biochemistry and genetics of this bacterial surface macromolecule, and (ii) to provide a basis for both vaccine development and virulence experiments. Both of these goals have been the driving force in studies of Yersinia LPS carried out during the last decade. Here we will review the progress made in the molecular genetics and biochemistry of Yersinia LPS. A deep understanding has been achieved with respect to Y. enterocolitica serotype O:3, reaching as far as a detailed analysis of the gene clusters directing the biosynthesis of the outer core oligosaccharide and of the O-ag. The O-ag gene clusters of Y. enterocolitica serotype O:8 and Y. pseudotuberculosis serotypes O:2a and O:5a have also been cloned and partially characterized LPS biosynthesis of these Yersinia species includes examples of the two major variations recognized in the biosynthesis of this macromolecule: (i) homopolymeric or O-antigen polymerase-independent biosynthesis, and (ii) heteropolymeric or O-antigen polymerase-dependent biosynthesis.
Lipopolysaccharide, genetic, gene, genetics, O-antigen, biochemistry, Yersinia, molecular genetics
Structure type: polymer chemical repeating unit
Location inside paper: p.858, Frame 8
Compound class: core oligosaccharide, O-antigen
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531
Biosynthesis and genetic data: genetic data
Comments, role: review
NCBI Taxonomy refs (TaxIDs): 630Reference(s) to other database(s): GTC:G15487QC
Show glycosyltransferases
There is only one chemically distinct structure:
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