Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
The structure was elucidated in this paperNCBI PubMed ID: 21752109Journal NLM ID: 8712028Publisher: Blackwell Publishing
Correspondence: strent
mail.utexas.edu
Institutions: Department of Biochemistry and Molecular Biology, Georgia Health Sciences University, Augusta, GA 30912, USA, Department of Chemistry and Biochemistry, Section of Molecular Genetics and Microbiology, The Institute of Cellular and Molecular Biology, The University of Texas at Austin, Austin, TX 78712, USA, South Texas Center for Emerging Infectious Diseases and Department of Biology, The University of Texas at San Antonio, San Antonio, TX 78249, USA
Similar to most Gram-negative bacteria, the outer leaflet of the outer membrane of Vibrio cholerae is comprised of lipopolysaccharide. Previous reports have proposed that V. cholerae serogroups O1 and O139 synthesize structurally different lipid A domains, which anchor lipopolysaccharide within the outer membrane. In the current study, intact lipid A species of V. cholerae O1 and O139 were analysed by mass spectrometry. We demonstrate that V. cholerae serogroups associated with human disease synthesize a similar asymmetrical hexa-acylated lipid A species, bearing a myristate (C14:0) and 3-hydroxylaurate (3-OH C12:0) at the 2'- and 3'-positions respectively. A previous report from our laboratory characterized the V. cholerae LpxL homologue Vc0213, which transfers a C14:0 to the 2'-position of the glucosamine disaccharide. Our current findings identify V. cholerae Vc0212 as a novel lipid A secondary hydroxy-acyltransferase, termed LpxN, responsible for transferring the 3-hydroxylaurate (3-OH C12:0) to the V. cholerae lipid A domain. Importantly, the presence of a 3-hydroxyl group on the 3'-linked secondary acyl chain was found to promote antimicrobial peptide resistance in V. cholerae; however, this functional group was not required for activation of the innate immune response.
Lipopolysaccharide, lipid A, mass spectrometry, Vibrio cholerae
Structure type: oligomer
Location inside paper: p.1321, fig.5 B
Compound class: lipid A
Contained glycoepitopes: IEDB_141806,IEDB_142488,IEDB_144998,IEDB_145002,IEDB_146664,IEDB_534864,IEDB_983931,SB_192
Methods: GC-MS, DNA techniques, GC, MALDI-TOF MS, genetic methods, CID-MS
Biosynthesis and genetic data: genetic data
Comments, role: major form penta-acylated lipid A.
Related record ID(s): 26217, 31143, 31144, 31145, 31146, 31147, 31148, 31149, 31150, 31151, 31152, 31153, 31155
NCBI Taxonomy refs (TaxIDs): 562
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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