ReviewMicrobiology and molecular biology reviews : MMBR1998
Acylation of Escherichia coli hemolysin: a unique protein lipidation mechanism underlying toxin function.
Review in Microbiology and molecular biology reviews : MMBR, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
63 citing papers in PubMed, 197 citations in OpenAlex.
- Folding of the nonacylated acylation domain of the adenylate cyclase toxin is templated by its C-terminal RTX domain.The Journal of biological chemistry · 2026Article
- Calcium-loaded acylated segment controls membrane penetration capacity of repeats-in-toxin cytolysins.The Journal of biological chemistry · 2026Article
- Insights into spatial dynamics of the microbiome and resistome across the conventional and organic dairy farms.PloS one · 2026Article
- The interaction ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Membrane Interaction Characteristics of the RTX Toxins and the Cholesterol-Dependence of Their Cytolytic/Cytotoxic Activity.International journal of molecular sciences · 2024Review
- UropathogenicMicroorganisms · 2023Review
- ppGpp, the General Stress Response Alarmone, Is Required for the Expression of the α-Hemolysin Toxin in the UropathogenicInternational journal of molecular sciences · 2022Article
- Review
- Characterization of virulence and antimicrobial resistance genes ofFrontiers in microbiology · 2022Article
- Genomic analysis of Shiga toxin-producing Escherichia coli O157:H7 from cattle and pork-production related environments.NPJ science of food · 2021Article
- Clostridium perfringens epsilon toxin binds to erythrocyte MAL receptors and triggers phosphatidylserine exposure.Journal of cellular and molecular medicine · 2020Article
- Article
- Review
- Review
- Aggregatibacter actinomycetemcomitans Leukotoxin (LtxA) Requires Death Receptor Fas, in Addition to LFA-1, To Trigger Cell Death in T Lymphocytes.Infection and immunity · 2019Article
- A new role for Zinc limitation in bacterial pathogenicity: modulation of α-hemolysin from uropathogenic Escherichia coli.Scientific reports · 2018Article
- Acinetobacter: an emerging pathogen with a versatile secretome.Emerging microbes & infections · 2018Review
- Protein Lipidation: Occurrence, Mechanisms, Biological Functions, and Enabling Technologies.Chemical reviews · 2018Article
- Acylation of the Type 3 Secretion System Translocon Using a Dedicated Acyl Carrier Protein.PLoS genetics · 2017Article
- Developmental origins of male subfertility: role of infection, inflammation, and environmental factors.Seminars in immunopathology · 2016Review
3 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
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The pore-forming hemolysin (HlyA) of Escherichia coli represents a unique class of bacterial toxins that require a posttranslational modification for activity. The inactive protoxin pro-HlyA is activated intracellularly by amide linkage of fatty acids to two internal lysine residues 126 amino acids apart, directed by the cosynthesized HlyC protein with acyl carrier protein as the fatty acid donor. This action distinguishes HlyC from all bacterial acyltransferases such as the lipid A, lux-specific, and nodulation acyltransferases, and from eukaryotic transferases such as N-myristoyl transferases, prenyltransferases, and thioester palmitoyltransferases. Most lipids directly attached to proteins may be classed as N-terminal amide-linked and internal ester-linked acyl groups and C-terminal ether-linked isoprenoid groups. The acylation of HlyA and related toxins does not equate to these but does appear related to a small number of eukaryotic proteins that include inflammatory cytokines and mitogenic and cholinergic receptors. While the location and structure of lipid moieties on proteins vary, there are common effects on membrane affinity and/or protein-protein interactions. Despite being acylated at two residues, HlyA does not possess a "double-anchor" motif and does not have an electrostatic switch, although its dependence on calcium binding for activity suggests that the calcium-myristoyl switch may have relevance. The acyl chains on HlyA may provide anchorage points onto the surface of the host cell lipid bilayer. These could then enhance protein-protein interactions either between HlyA and components of a host signal transduction pathway to influence cytokine production or between HlyA monomers to bring about oligomerization during pore formation.
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Registered trials
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.