Function and Biogenesis of Lipopolysaccharides

Bertani, Blake; Ruiz, Natividad

doi:10.1128/ecosalplus.esp-0001-2018

Cited by 742Bacterial Genetics and BiotechnologyEscherichia coli research studiesImmune Response and Inflammation

Function and Biogenesis of Lipopolysaccharides

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Bertani, Blake, Ruiz, Natividad·2018·EcoSal Plus

DOI 10.1128/ecosalplus.esp-0001-2018PMC PMC6091223

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Abstract

The cell envelope is the first line of defense between a bacterium and the world-at-large. Often, the initial steps that determine the outcome of chemical warfare, bacteriophage infections, and battles with other bacteria or the immune system greatly depend on the structure and composition of the bacterial cell surface. One of the most studied bacterial surface molecules is the glycolipid known as lipopolysaccharide (LPS), which is produced by most Gram-negative bacteria. Much of the initial attention LPS received in the early 1900s was owed to its ability to stimulate the immune system, for which the glycolipid was commonly known as endotoxin. It was later discovered that LPS also creates a permeability barrier at the cell surface and is a main contributor to the innate resistance that Gram-negative bacteria display against many antimicrobials. Not surprisingly, these important properties of LPS have driven a vast and still prolific body of literature for more than a hundred years. LPS research has also led to pioneering studies in bacterial envelope biogenesis and physiology, mostly using Escherichia coli and Salmonella as model systems. In this review, we will focus on the fundamental knowledge we have gained from studies of the complex structure of the LPS molecule and the biochemical pathways for its synthesis, as well as the transport of LPS across the bacterial envelope and its assembly at the cell surface.

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Among genes involved in bacterial LPS assembly, lpxA, B, C, D, H, K and wdtA/waaA encode genes required for basic LPS assembly and tetra-acylation of lipid A, whereas lpxL facilitates LPS penta-acylation, and lpxJ and lpxM hexa-acylate LPS with differing acyl chain lengths and positions.
“Among genes involved in bacterial LPS assembly, lpxA, B, C, D, H, K and wdtA/waaA encode genes required for basic LPS assembly and tetra-acylation of lipid A, whereas lpxL facilitates LPS penta-acylation, and lpxJ and lpxM hexa-acylate LPS with differing acyl chain lengths and positions14,15.”
From Gut microbiota-derived hexa-acylated lipopolysaccharides enhance cancer immunotherapy responses (2025) · cites this paper as [14]

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Comparative functional characterization in vitro of heptosyltransferase I (WaaC) and II (WaaF) from Escherichia coli
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Hydrocarbon Rulers in UDP-N-acetylglucosamine Acyltransferases
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Two-Component Signaling and Gram Negative Envelope Stress Response Systems
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Molecular cloning of the genes for lipid A disaccharide synthase and UDP-N-acetylglucosamine acyltransferase in Escherichia coli
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LptE binds to and alters the physical state of LPS to catalyze its assembly at the cell surface
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Structures of the rfaB, rfaI, rfaJ, and rfaS genes of Escherichia coli K-12 and their roles in assembly of the lipopolysaccharide core
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Molecular and Structural Basis of Inner Core Lipopolysaccharide Alterations in Escherichia coli
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Accumulation of the Lipid A Precursor UDP-2,3-diacylglucosamine in an Escherichia coli Mutant Lacking the lpxH Gene
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Burkholderia cenocepacia O antigen lipopolysaccharide prevents phagocytosis by macrophages and adhesion to epithelial cells
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Ca2+-induced Phosphoethanolamine Transfer to the Outer 3-Deoxy-d-manno-octulosonic Acid Moiety of Escherichia coli Lipopolysaccharide
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The Active Site of Escherichia coli UDP-N-acetylglucosamine Acyltransferase
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Biosynthesis of lipid A in Escherichia coli: identification of UDP-3-O-[(R)-3-hydroxymyristoyl]-.alpha.-D-glucosamine as a precursor of UDP-N2,O3-bis[(R)-3-hydroxymyristoyl]-.alpha.-D-glucosamine
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The biosynthesis of gram-negative endotoxin. A novel kinase in Escherichia coli membranes that incorporates the 4'-phosphate of lipid A.
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Purification and properties of lipid A disaccharide synthase of Escherichia coli.
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Dual Role of FtsH in Regulating Lipopolysaccharide Biosynthesis in Escherichia coli
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An Inner Membrane Dioxygenase that Generates the 2-Hydroxymyristate Moiety of Salmonella Lipid A
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Glucosamine Found as a Substituent of Both Phosphate Groups inBordetellaLipid A Backbones: Role of a BvgAS-Activated ArnT Ortholog
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Accumulation of a Lipid A Precursor Lacking the 4′-Phosphate following Inactivation of the Escherichia coli lpxKGene
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Steady-State Kinetics and Mechanism of LpxD, the N -Acyltransferase of Lipid A Biosynthesis
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O Antigen Protects Bordetella parapertussis from Complement
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Enzymatic Modification of Lipid A by ArnT Protects Bordetella bronchiseptica against Cationic Peptides and Is Required for Transmission
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Gut microbiome and health: mechanistic insights
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Authors: Bertani, B., & Ruiz, N.
Affiliations: The Ohio State University (US)
Corresponding author: Ruiz, Natividad
ORCID: Ruiz, Natividad
Venue: EcoSal Plus
Publisher: American Society for Microbiology
Published: 2018-12-31
Volume: 8
Issue: 1
ISSN: 2324-6200 (ISSN-L)
DOI: 10.1128/ecosalplus.esp-0001-2018
PMC: PMC6091223
OpenAlex: W2885761488
Cited by: 742
References: 174
Citations by year: 2026: 86 · 2025: 126 · 2024: 140 · 2023: 135 · 2022: 122 · 2021: 92 · 2020: 31 · 2019: 8 · 2018: 1
FWCI: 20.19
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: EcoSal Plus (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
Funders: National Institutes of Health
National Institute of General Medical Sciences (R01GM100951)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Escherichia coli research studies
Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Keywords: lipopolysaccharide, Gram-negative bacteria, bacterial cell envelope, endotoxin, LPS structure, Escherichia coli, Salmonella
MeSH terms: Bacterial Outer Membrane Proteins, Biological Transport, Cell Membrane, Cell Wall, Escherichia coli, Gram-Negative Bacteria, Lipid A, Lipopolysaccharides, Models, Biological, Escherichia coli Proteins, Biosynthetic Pathways

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