ArticleBiochemistry2010
Interchangeable domains in the Kdo transferases of Escherichia coli and Haemophilus influenzae.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 43 citations in OpenAlex.
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- Effect of Glycosylation on Self-Assembly of Lipid A Lipopolysaccharides in Aqueous Solutions.Langmuir : the ACS journal of surfaces and colloids · 2023Article
- Structural basis for the toxic activity of MafB2 from maf genomic island 2 (MGI-2) in N. meningitidis B16B6.Scientific reports · 2023Article
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- An antibacterial T6SS in Pantoea agglomerans pv. betae delivers a lysozyme-like effector to antagonize competitors.Environmental microbiology · 2022Article
- Exploring a combined Escherichia coli-based glycosylation and in vitro transglycosylation approach for expression of glycosylated interferon alpha.Bioorganic & medicinal chemistry · 2021Article
- Metabolic engineering of Escherichia coli to produce a monophosphoryl lipid A adjuvant.Metabolic engineering · 2020Article
- Interplay between mitochondria and diet mediates pathogen and stress resistance in Caenorhabditis elegans.PLoS genetics · 2019Article
- Biochemical and Structural Insights into an Fe(II)/α-Ketoglutarate/OJournal of molecular biology · 2018Article
- Crystal structure and activity of Francisella novicida UDP-N-acetylglucosamine acyltransferase.Biochemical and biophysical research communications · 2016Article
- Kdo hydroxylase is an inner core assembly enzyme in the Ko-containing lipopolysaccharide biosynthesis.Biochemical and biophysical research communications · 2014Article
- Structural basis of lipid binding for the membrane-embedded tetraacyldisaccharide-1-phosphate 4'-kinase LpxK.The Journal of biological chemistry · 2014Article
- Mutants resistant to LpxC inhibitors by rebalancing cellular homeostasis.The Journal of biological chemistry · 2013Article
- Structural and mechanistic analysis of the membrane-embedded glycosyltransferase WaaA required for lipopolysaccharide synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Three phosphatidylglycerol-phosphate phosphatases in the inner membrane of Escherichia coli.The Journal of biological chemistry · 2011Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Kdo(2)-lipid A, a conserved substructure of lipopolysaccharide, plays critical roles in Gram-negative bacterial survival and interaction with host organisms. Inhibition of Kdo biosynthesis in Escherichia coli results in cell death and accumulation of the tetra-acylated precursor lipid IV(A). E. coli KdtA (EcKdtA) is a bifunctional enzyme that transfers two Kdo units from two CMP-Kdo molecules to lipid IV(A). In contrast, Haemophilus influenzae KdtA (HiKdtA) transfers only one Kdo unit. E. coli CMR300, which lacks Kdo transferase because of a deletion in kdtA, can be rescued to grow in broth at 37 degrees C if multiple copies of msbA are provided in trans. MsbA, the inner membrane transporter for nascent lipopolysaccharide, prefers hexa-acylated to tetra-acylated lipid A, but with the excess MsbA present in CMR300, lipid IV(A) is efficiently exported to the outer membrane. CMR300 is hypersensitive to hydrophobic antibiotics and bile salts and does not grow at 42 degrees C. Expressing HiKdtA in CMR300 results in the accumulation of Kdo-lipid IV(A) in place of lipid IV(A) without suppression of its growth phenotypes at 30 degrees C. EcKdtA restores intact lipopolysaccharide, together with normal antibiotic resistance, detergent resistance, and growth at 42 degrees C. To determine which residues are important for the mono- or bifunctional character of KdtA, protein chimeras were constructed using EcKdtA and HiKdtA. These chimeras, which are catalytically active, were characterized by in vitro assays and in vivo complementation. The N-terminal half of KdtA, especially the first 30 amino acid residues, specifies whether one or two Kdo units are transferred to lipid IV(A).
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