ArticleJournal of bacteriology2005
Mutations in HlyD, part of the type 1 translocator for hemolysin secretion, affect the folding of the secreted toxin.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- TolC Is Required for a Mixed-Linkage β-Glucan (MLG) Biosynthesis: Engineering Bacteria for MLG Overproduction.Microbial biotechnology · 2026Article
- Reducing the sensitivity of Halomonas sp. to oxygen availability through adaptive laboratory evolution.Microbial cell factories · 2026Article
- Molecular typing and virulence characteristics of Escherichia coli strains isolated from hospital and community acquired urinary tract infections.Molecular biology reports · 2024Article
- Development of a candidate multi-epitope vaccine againstSaudi medical journal · 2023Article
- Review
- Whole genome sequencing of the multidrug-resistantFrontiers in medicine · 2022Article
- Genomic Insights into Drug Resistance Determinants inMicroorganisms · 2021Article
- Adaptive Interactions ofPathogens (Basel, Switzerland) · 2021Article
- Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria.Chemical reviews · 2021Review
- Gut Microbial SNPs Induced by High-Fiber Diet Dominate Nutrition Metabolism and Environmental Adaption ofFrontiers in microbiology · 2021Article
- Nonfimbrial Adhesin Mutants Reveal DivergentInternational journal of microbiology · 2021Article
- Functional Seasonality of Free-Living and Particle-Associated Prokaryotic Communities in the Coastal Adriatic Sea.Frontiers in microbiology · 2020Article
- Screening and purification of nanobodies from E. coli culture supernatants using the hemolysin secretion system.Microbial cell factories · 2019Article
- Structural and functional dissection reveals distinct roles of Ca2+-binding sites in the giant adhesin SiiE of Salmonella enterica.PLoS pathogens · 2017Article
- Diversity ofFrontiers in microbiology · 2017Article
- Type I Protein Secretion-Deceptively Simple yet with a Wide Range of Mechanistic Variability across the Family.EcoSal Plus · 2016Review
- The Human Pathogen Streptococcus pyogenes Releases Lipoproteins as Lipoprotein-rich Membrane Vesicles.Molecular & cellular proteomics : MCP · 2015Article
- Novel mixed-linkage β-glucan activated by c-di-GMP in Sinorhizobium meliloti.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Article
- Architecture and roles of periplasmic adaptor proteins in tripartite efflux assemblies.Frontiers in microbiology · 2015Review
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5 authors.
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Abstract
HlyD, a member of the membrane fusion protein family, is essential for the secretion of the RTX hemolytic toxin HlyA from Escherichia coli. Random point mutations affecting HlyA secretion were obtained, distributed in most periplasmic regions of the HlyD molecule. Analysis of the secretion phenotypes of different mutants allowed the identification of regions in HlyD involved in different steps of HlyA translocation. Four mutants, V349-I, T85-I, V334-I and L165-Q, were conditionally defective, a phenotype shown to be linked to the presence of inhibitory concentrations of Ca2+ in extracellular medium. Hly mutant T85-I was defective at an early stage in secretion, while mutants V334-I and L165-Q appeared to accumulate HlyA in the cell envelope, indicating a block at an intermediate step. Mutants V349-I, V334-I, and L165-Q were only partially defective in secretion, allowing significant levels of HlyA to be transported, but in the case of V349-I and L165-Q the HlyA molecules secreted showed greatly reduced hemolytic activity. Hemolysin molecules secreted from V349-I and V334-I are defective in normal folding and can be reactivated in vitro to the same levels as HlyA secreted from the wild-type translocator. Both V349-I and V334-I mutations mapped to the C-terminal lipoyl repeat motif, involved in the switching from the helical hairpin to the extended form of HlyD during assembly of the functional transport channel. These results suggest that HlyD is an integral component of the transport pathway, whose integrity is essential for the final folding of secreted HlyA into its active form.
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