ArticleCell reports2022
Caulobacter lipid A is conditionally dispensable in the absence of fur and in the presence of anionic sphingolipids.
Article in Cell reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 24 citations in OpenAlex.
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- Van der Waals interactions mediate the enantiomeric substrate preference of the CTP:phosphoglycerate cytidylyltransferase CpgD.bioRxiv : the preprint server for biology · 2026Article
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- A conserved hub protein required for peptidoglycan remodeling and cell division inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Sphingolipid-mediated vesiculation in multidrug-resistantApplied and environmental microbiology · 2025Article
- An N4-likebioRxiv : the preprint server for biology · 2025Article
- A co-conserved gene pair supportsJournal of bacteriology · 2025Article
- A co-conserved gene pair supportsbioRxiv : the preprint server for biology · 2025Article
- Genes required for phosphosphingolipid formation in Caulobacter crescentus contribute to bacterial virulence.PLoS pathogens · 2024Article
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- Mapping the IscR regulon sheds light on the regulation of iron homeostasis inFrontiers in microbiology · 2024Article
- Effects of Lead and Cadmium Combined Heavy Metals on Liver Function and Lipid Metabolism in Mice.Biological trace element research · 2023Article
- Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: An update for 2021-2022.Mass spectrometry reviewsReview
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10 authors at 5 institutions in 2 countries.
Funding
Abstract
Lipid A, the membrane-anchored portion of lipopolysaccharide (LPS), is an essential component of the outer membrane (OM) of nearly all Gram-negative bacteria. Here we identify regulatory and structural factors that together render lipid A nonessential in Caulobacter crescentus. Mutations in the ferric uptake regulator fur allow Caulobacter to survive in the absence of either LpxC, which catalyzes an early step of lipid A synthesis, or CtpA, a tyrosine phosphatase homolog we find is needed for wild-type lipid A structure and abundance. Alterations in Fur-regulated processes, rather than iron status per se, underlie the ability to survive when lipid A synthesis is blocked. Fitness of lipid A-deficient Caulobacter requires an anionic sphingolipid, ceramide phosphoglycerate (CPG), which also mediates sensitivity to the antibiotic colistin. Our results demonstrate that, in an altered regulatory landscape, anionic sphingolipids can support the integrity of a lipid A-deficient OM.
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