ArticleInfection and immunity2002
Modification of the structure and activity of lipid A in Yersinia pestis lipopolysaccharide by growth temperature.
Article in Infection and immunity, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 119 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
119 citing papers in PubMed, 241 citations in OpenAlex.
- Bacterial lipid structural diversity mediates commensalism and pathogenesis.Nature reviews. Microbiology · 2026Review
- Outer membrane engineering through lipid A modification allows modulation ofInfection and immunity · 2026Article
- Gut microbiota-derived hexa-acylated lipopolysaccharides enhance cancer immunotherapy responses.Nature microbiology · 2025Article
- Pathogenicity and virulence ofVirulence · 2024Review
- Diversity, Complexity, and Specificity of Bacterial Lipopolysaccharide (LPS) Structures Impacting Their Detection and Quantification.International journal of molecular sciences · 2024Article
- Towards a Yersinia pestis lipid A recreated in an Escherichia coli scaffold genome.Access microbiology · 2024Article
- Structure Determination of Lipid A with Multiple Glycosylation Sites by Tandem MS of Lithium-Adducted Negative Ions.Journal of the American Society for Mass Spectrometry · 2023Article
- Heterogeneity of Lipopolysaccharide as Source of Variability in Bioassays and LPS-Binding Proteins as Remedy.International journal of molecular sciences · 2023Review
- Lipid A structural diversity among members of the genusFrontiers in microbiology · 2023Article
- Article
- Intact polar lipidome and membrane adaptations of microbial communities inhabiting serpentinite-hosted fluids.Frontiers in microbiology · 2023Article
- A highly immunogenic vaccine platform against encapsulated pathogens using chimeric probiotic Escherichia coli membrane vesicles.NPJ vaccines · 2022Article
- Position-Specific Secondary Acylation Determines Detection of Lipid A by Murine TLR4 and Caspase-11.Infection and immunity · 2022Article
- Subversion of GBP-mediated host defense by E3 ligases acquired during Yersinia pestis evolution.Nature communications · 2022Article
- Plague Outbreak of aVector borne and zoonotic diseases (Larchmont, N.Y.) · 2022Article
- Force spectroscopy of interactions between Yersinia pseudotuberculosis and Yersinia pestis cells and monoclonal antibodies using optical tweezers.European biophysics journal : EBJ · 2022Article
- Lipid A heterogeneity and its role in the host interactions with pathogenic and commensal bacteria.microLife · 2022Review
- Article
- Lipid A-Mediated Bacterial-Host Chemical Ecology: Synthetic Research of Bacterial Lipid As and Their Development as Adjuvants.Molecules (Basel, Switzerland) · 2021Review
- Lipopolysaccharide of theBiomolecules · 2021Review
59 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Yersinia pestis strain Yreka was grown at 27 or 37 degrees C, and the lipid A structures (lipid A-27 degrees C and lipid A-37 degrees C) of the respective lipopolysaccharides (LPS) were investigated by matrix-assisted laser desorption ionization-time-of-flight (MALDI-TOF) mass spectrometry. Lipid A-27 degrees C consisted of a mixture of tri-acyl, tetra-acyl, penta-acyl, and hexa-acyl lipid A's, of which tetra-acyl lipid A was most abundant. Lipid A-37 degrees C consisted predominantly of tri- and tetra-acylated molecules, with only small amounts of penta-acyl lipid A; no hexa-acyl lipid A was detected. Furthermore, the amount of 4-amino-arabinose was substantially higher in lipid A-27 degrees C than in lipid A-37 degrees C. By use of mouse and human macrophage cell lines, the biological activities of the LPS and lipid A preparations were measured via their abilities to induce production of tumor necrosis factor alpha (TNF-alpha). In both cell lines the LPS and the lipid A from bacteria grown at 27 degrees C were stronger inducers of TNF-alpha than those from bacteria grown at 37 degrees C. However, the difference in activity was more prominent in human macrophage cells. These results suggest that in order to reduce the activation of human macrophages, it may be more advantageous for Y. pestis to produce less-acylated lipid A at 37 degrees C.
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Registered trials
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