ArticleJournal of bacteriology1996
Analysis of the in vivo activation of hemolysin (HlyA) from Escherichia coli.
Article in Journal of bacteriology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 74 citations in OpenAlex.
- Uncommon Pathogens in Common Presentations: Genetic Profiling and Virulence Determinants ofInfectious disease reports · 2025Article
- Heterologously secreted MbxA from Moraxella bovis induces a membrane blebbing response of the human host cell.Scientific reports · 2022Article
- Review
- Lysine Fatty Acylation: Regulatory Enzymes, Research Tools, and Biological Function.Frontiers in cell and developmental biology · 2021Review
- Acyltransferase-mediated selection of the length of the fatty acyl chain and of the acylation site governs activation of bacterial RTX toxins.The Journal of biological chemistry · 2020Article
- Aggregatibacter actinomycetemcomitans leukotoxin: From mechanism to targeted anti-toxin therapeutics.Molecular oral microbiology · 2020Review
- Channel Formation by LktA ofToxins · 2019Article
- Cytotoxic activity of Kingella kingae RtxA toxin depends on post-translational acylation of lysine residues and cholesterol binding.Emerging microbes & infections · 2018Article
- Type 1 Does the Two-Step: Type 1 Secretion Substrates with a Functional Periplasmic Intermediate.Journal of bacteriology · 2018Review
- Structure of a bacterial toxin-activating acyltransferase.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Article
- Acyltransferases in bacteria.Microbiology and molecular biology reviews : MMBR · 2013Review
- Aggregatibacter actinomycetemcomitans leukotoxin is post-translationally modified by addition of either saturated or hydroxylated fatty acyl chains.Molecular oral microbiology · 2011Article
- RTX proteins: a highly diverse family secreted by a common mechanism.FEMS microbiology reviews · 2010Review
- Interaction between leukotoxin and Cu,Zn superoxide dismutase in Aggregatibacter actinomycetemcomitans.Infection and immunity · 2007Article
- Highly divergent RfaH orthologs from pathogenic proteobacteria can substitute for Escherichia coli RfaH both in vivo and in vitro.Journal of bacteriology · 2004Article
- Characterization of Escherichia coli isolates incriminated in colisepticaemia in mink.Veterinary research communications · 2003Article
- Isolation and characterization of Escherichia coli tolC mutants defective in secreting enzymatically active alpha-hemolysin.Journal of bacteriology · 2001Article
- Hemolytically active (acylated) alpha-hemolysin elicits interleukin-1beta (IL-1beta) but augments the lethality of Escherichia coli by an IL-1- and tumor necrosis factor-independent mechanism.Infection and immunity · 1998Article
- Acylation of Escherichia coli hemolysin: a unique protein lipidation mechanism underlying toxin function.Microbiology and molecular biology reviews : MMBR · 1998Review
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hemolysin (HlyA) from Escherichia coli containing the hlyCABD operon separated from the nonhemolytic pro-HlyA upon two-dimensional (2-D) polyacrylamide gel electrophoresis. The migration distance indicated a net loss of two positive charges in HlyA as a result of the HlyC-mediated activation (modification). HlyA activated in vitro in the presence of [U-14C]palmitoyl-acyl carrier protein comigrated with in vivo-activated hemolysin on 2-D gels and was specifically labelled, in agreement with the assumption that the activation is accomplished in vitro and in vivo by covalent fatty acid acylation. The in vivo-modified amino acid residues were identified by peptide mapping and 2-D polyacrylamide gel electrophoresis of mutant and truncated HlyA derivatives, synthesized in E. coli in the presence and absence of HlyC. These analyses indicated that the internal residues Lys-564 and Lys-690 of HlyA, which have recently been shown by others to be fatty acid acylated by HlyC in vitro, are also the only modification sites in vivo. HlyA activated in E. coli was quantitatively fatty acid acylated at both sites, and the double modification was required for wild-type hemolytic activity. Single modifications in mutant and truncated HlyA derivatives suggested that both lysine residues are independently fatty acid acylated by a mechanism requiring additional sequences or structures flanking the corresponding acylation site. The intact repeat domain of HlyA was not required for the activation. The pore-forming activities of pro-HlyA and singly modified HlyA mutants in planar lipid bilayer membranes suggested that the activation is not essential for transmembrane pore formation but rather required for efficient binding of the toxin to target membranes.
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