ArticleApplied and environmental microbiology2013
Dual roles of Pseudomonas aeruginosa AlgE in secretion of the virulence factor alginate and formation of the secretion complex.
Article in Applied and environmental microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 32 citations in OpenAlex.
- Structural basis of the AlgU-MucAmBio · 2026Article
- Integrated computational and experimental evaluation of natural products targeting PGM/AlgC and HisIE in multidrug-resistant respiratory pathogens.Frontiers in microbiology · 2026Article
- Rhizosphere bacterial exopolysaccharides: composition, biosynthesis, and their potential applications.Archives of microbiology · 2024Review
- Article
- Alginate-like exopolysaccharides extracted from different waste sludges exhibit varying physicochemical and material properties.Frontiers in microbiology · 2024Article
- Pseudomonas aeruginosa biofilm exopolysaccharides: assembly, function, and degradation.FEMS microbiology reviews · 2023Review
- Structure of the AlgKX modification and secretion complex required for alginate production and biofilm attachment in Pseudomonas aeruginosa.Nature communications · 2022Article
- Extracellular Polymeric Substances and Biocorrosion/Biofouling: Recent Advances and Future Perspectives.International journal of molecular sciences · 2022Review
- Zymomonas diversity and potential for biofuel production.Biotechnology for biofuels · 2021Article
- Physicochemical Properties of Extracellular Polymeric Substances Produced by Three Bacterial Isolates From Biofouled Reverse Osmosis Membranes.Frontiers in microbiology · 2021Article
- Article
- Bioengineering a bacterial pathogen to assemble its own particulate vaccine capable of inducing cellular immunity.Scientific reports · 2017Article
- Biological function of a polysaccharide degrading enzyme in the periplasm.Scientific reports · 2016Article
- Alginate Biosynthesis Factories in Pseudomonas fluorescens: Localization and Correlation with Alginate Production Level.Applied and environmental microbiology · 2016Article
- Properties and Phylogeny of 76 Families of Bacterial and Eukaryotic Organellar Outer Membrane Pore-Forming Proteins.PloS one · 2016Article
- Bacterial cellulose biosynthesis: diversity of operons, subunits, products, and functions.Trends in microbiology · 2015Review
- Article
- Bacterial exopolysaccharides: biosynthesis pathways and engineering strategies.Frontiers in microbiology · 2015Review
- Microbial alginate production, modification and its applications.Microbial biotechnology · 2013Review
- Insights into the assembly of the alginate biosynthesis machinery in Pseudomonas aeruginosa.Applied and environmental microbiology · 2013Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
AlgE is a monomeric 18-stranded β-barrel protein required for secretion of the extracellular polysaccharide alginate in Pseudomonas aeruginosa. To assess the molecular mechanism of alginate secretion, AlgE was subjected to site-specific and FLAG epitope insertion mutagenesis. Except for β-strands 6 and 10, epitope insertions into the transmembrane β-strands abolished localization of AlgE to the outer membrane. Interestingly, an epitope insertion into β-strand 10 produced alginate and was only detectable in outer membranes isolated from cells grown on solid media. The deletion of nine C-terminal amino acid residues destabilized AlgE. Replacement of amino acids that constitute the highly electropositive pore constriction showed that individual amino acid residues have a specific function in alginate secretion. Two of the triple mutants (K47E+R353A+R459E and R74E+R362A+R459E) severely reduced alginate production. Mutual stability analysis using the algE deletion mutant PDO300ΔalgE(miniCTX) showed the periplasmic alginate biosynthesis proteins AlgK and AlgX were completely destabilized, while the copy number of the inner membrane c-di-GMP receptor Alg44 was reduced. Chromosomal integration of algE restored AlgK, AlgX, and Alg44, providing evidence for a multiprotein complex that spans the cell envelope. Periplasmic turn 4 of AlgE was identified as an important region for maintaining the stability of the putative multiprotein complex.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.