ArticleMolecular & cellular proteomics : MCP2013
Analysis of Soluble protein complexes in Shigella flexneri reveals the influence of temperature on the amount of lipopolysaccharide.
Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 15 citations in OpenAlex.
- Characterization ofmBio · 2025Article
- Bacterial lysis or survival after infection with phage Sf14 depends on combined nutrient and temperature conditions.PloS one · 2025Article
- TheApplied and environmental microbiology · 2024Article
- Host Range Expansion ofJournal of virology · 2022Article
- How doesWorld journal of gastroenterology · 2019Review
- UV-C Adaptation of Shigella: Morphological, Outer Membrane Proteins, Secreted Proteins, and Lipopolysaccharides Effects.Current microbiology · 2017Article
- Role of the virulence plasmid in acid resistance of Shigella flexneri.Scientific reports · 2017Article
- An H-NS Family Protein, Sfh, Regulates Acid Resistance by Inhibition of Glutamate Decarboxylase Expression inFrontiers in microbiology · 2017Article
- Intracellular Shigella remodels its LPS to dampen the innate immune recognition and evade inflammasome activation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
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11 authors at 3 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Shigella flexneri, which is closely related to Escherichia coli, is the most common cause of the endemic form of shigellosis. In this study, 53 homomultimeric protein complexes and nine heteromultimeric protein complexes from S. flexneri 2a strain 2457T were separated and identified. Among these, three potential homomultimeric protein complexes had not been previously described. One complex, thought to be composed of 12 PhoN1 subunits, is a periplasmic protein with an unknown physiological role encoded on the virulence plasmid of S. flexneri. The abundance of the protein complexes was compared following growth at 37 or 30°C, and the abundance of three protein complexes (PyrB-PyrI, GlmS, and MglB) related to the synthesis of lipopolysaccharides (LPS) appeared to be temperature-dependent. Many studies have shown that LPS is essential to the virulence of S. flexneri. Here, we report the influence of temperature on the amount of LPS.
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