Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 22353600Publication DOI: 10.1111/j.1365-2672.2012.05263Journal NLM ID: 9706280Publisher: Oxford: Blackwell Publishing for the Society for Applied Bacteriology
Correspondence: xiaoyuanwang

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Institutions: State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, China
AIMS: To investigate the role of lipopolysaccharide (LPS) structure in the stability of outer membrane and the ability of biofilm formation in Cronobacter sakazakii. METHODS AND RESULTS: A C. sakazakii mutant strain LWW02 was constructed by inactivating the gene ESA_04107 encoding for heptosyltransferase I. LPS were purified from LWW02, and changes in their structure were confirmed by thin-layer chromatography and electrospray ionization mass spectrometry. Comparing with the wild-type strain BAA-894, slower growth, higher membrane permeability, higher surface hydrophobicity, stronger ability of autoaggregation and biofilm formation were observed for the mutant strain LWW02. CONCLUSIONS: The gene ESA_04107 encodes heptosyltransferase I in C. sakazakii ATCC BAA-894. The cleavage of LPS in C. sakazakii could cause its outer membrane defects and increase its ability to form biofilms. SIGNIFICANCE AND IMPACT OF THE STUDY: The study is important for understanding the pathogenic mechanism and efficient control of C. sakazakii.
Lipopolysaccharide, biosynthesis, outer membrane, biofilms, WaaC, Cronobacter sakazakii
Structure type: oligomer
Location inside paper: p.986, fig.1
Compound class: core oligosaccharide, LPS
Contained glycoepitopes: IEDB_130650,IEDB_130659,IEDB_135394,IEDB_135515,IEDB_141807,IEDB_150908,IEDB_151531,IEDB_176772,IEDB_2189047,IEDB_534864
Methods: SDS-PAGE, DNA techniques, TLC, ESI-MS, genetic methods, electron microscopy
Enzymes that release or process the structure: WaaC heptosyltransferase I
Related record ID(s): 29382
NCBI Taxonomy refs (TaxIDs): 562
Show glycosyltransferases
There is only one chemically distinct structure: