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Taxonomic group: bacteria / Proteobacteria (Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11: XN6P4

]

NCBI PubMed ID: 19346244
Publication DOI: 10.1074/jbc.M900490200
Journal NLM ID: 2985121R
Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: sraina

fz-borstel.de
Institutions: From the Research Center Borstel, Leibniz-Center for Medicine and Biosciences, Borstel, Germany

To elucidate the minimal lipopolysaccharide (LPS) structure needed for the viability of Escherichia coli, suppressor-free strains lacking either 3-deoxy-D-manno-oct-2-ulosonic acid transferase waaA gene or derivatives of heptosyltransferase I waaC deletion with lack of one or all late acyltransferases (lpxL/M/P) and/or various outer membrane biogenesis factors were constructed. ∆(waaClpxLlpxMlpxP) and waaA mutants exhibited highly attenuated growth, whereas simultaneous deletion of waaC and surA was lethal. Analyses of LPS of suppressor-free waaA mutants grown at 21(R)C, besides showing accumulation of free lipid IV(A) precursor, also revealed the presence of its pentaacylated and hexaacylated derivatives, indicating in vivo late acylation can occur without Kdo. In contrast, LPS of ∆(waaClpxLlpxMlpxP) strains showed primarily Kdo(2)-lipid IV(A), indicating that these minimal LPS structures are sufficient to support growth of E. coli under slow-growth conditions at 21(0)C. These lipid IV(A) derivatives could be modified biosynthetically by phosphoethanolamine, but not by 4-amino-4-deoxy-L-arabinose, indicating export defects of such minimal LPS. ∆waaA and ∆(waaClpxLlpxMlpxP) exhibited cell-division defects with a decrease in the levels of FtsZ and OMP-folding factor PpiD. These mutations led to strong constitutive additive induction of envelope responsive CpxR/A and sigma(E) signal transduction pathways. ∆(lpxLlpxMlpxP) mutant, with intact waaC, synthesized tetraacylated lipid A and constitutively incorporated a third Kdo in growth medium inducing synthesis of P-EtN and L-Ara4N. Overexpression of msbA restored growth of ∆(lpxLlpxMlpxP) under fast-growing conditions, but only partially that of ∆(waaClpxLlpxMlpxP) mutant. This suppression could be alleviated by overexpression of certain mutant msbA alleles or by single-copy chromosomal MsbA-498V variant in the vicinity of Walker-boxII.

lipid A, glycosyltransferases, lipopolysaccharide structure, outer membrane, acyltransferases, stress, Escherichia coli K12

Structure type: oligomer
Location inside paper: p.15375, fig.3B, Kdo2-lipid IVA
Compound class: lipid A
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_135394,IEDB_135515,IEDB_141181,IEDB_141807,IEDB_150908,IEDB_151531,IEDB_176772,IEDB_534864

Methods: PCR, TLC, acid hydrolysis, ESI-ICR-MS, Western blotting, genetic methods, enzyme assay
Biosynthesis and genetic data: genetic data
Comments, role: LIP = C16:1

Related record ID(s): 23741
NCBI Taxonomy refs (TaxIDs): 83333
Show glycosyltransferases

There is only one chemically distinct structure:

[1*]O[C@H](CCCCCCCCCCC)CC(=O)N[C@H]1[C@H](OC[C@H]2O[C@H](OP(=O)(O)OP(=O)(O)OCCN)[C@H](NC(=O)C[C@@H](CCCCCCCCCCC)OC(=O)CCCCCCCCCCCCCCC)[C@@H](OC(=O)C[C@H](O)CCCCCCCCCCC)[C@@H]2O)O[C@H](CO[C@]2(C(=O)O)C[C@@H](O[C@]3(C(=O)O)C[C@@H](O)[C@@H](O)[C@@H]([C@@H](CO)OP(=O)(O)OCCN)O3)[C@@H](O)[C@@H]([C@H](O)CO)O2)[C@@H](OP(=O)(O)OC2OC[C@H](N)[C@H](O)[C@H]2O)[C@@H]1OC(=O)C[C@@H](CCCCCCCCCCC)OC(=O)CCCCCCCCCCCCC

SVG MW SMILES 3D mol Ionize

R1 = LIP