E.coli hemolysin interactions with prokaryotic and eukaryotic cell membranes
- 1 August 1992
- Vol. 14 (8) , 519-525
- https://doi.org/10.1002/bies.950140804
Abstract
The hemolysin toxin (HlyA) is secreted across both the cytoplasmic and outer membranes of pathogenic Escherichia coli and forms membrane pores in cells of the host immune system, causing cell dysfunction and death. The processes underlying the interaction of HlyA with the bacterial and mammalian cell membranes are remarkable. Secretion of HlyA occurs without a periplasmic intermediate and is directed by an uncleaved C‐terminal targetting signal and the HlyB and HlyD translocator proteins, the former being a member of a transporter superfamily central to import and export of a wide range of substrates by prokaryotic and eukaryotic cells. The separate process by which HlyA is targetted to mammalian cell membranes is dependent upon fatty acylation of a non‐toxic precursor, proHlyA. This is achieved by a novel mechanism directed by the activator protein HlyC, which binds to an internal proHlyA recognition sequence and provides specificity for the transfer of fatty acid from cellular acyl carrier protein.Keywords
This publication has 51 references indexed in Scilit:
- Escherichia coli HIyT protein, a transcriptional activator of haemolysin synthesis and secretion, is encoded by the rfaH (sfrB) locus required for expression of sex factor and lipopolysaccharide genesMolecular Microbiology, 1992
- Secretion of the Rhizobium leguminosarum nodulation protein NodO by haemolysin‐type systemsMolecular Microbiology, 1992
- Mutational analysis supports a role for multiple structural features in the C‐terminal secretion signal of Escherichia coli haemolysinMolecular Microbiology, 1991
- Analysis of the membrane organization of an Escherichia coli protein translocator, HlyB, a member of a large family of prokaryote and eukaryote surface transport proteinsJournal of Molecular Biology, 1991
- A yeast mitochondrial outer membrane protein essential for protein import and cell viabilityNature, 1990
- Symbiotic host-specificity of Rhizobium meliloti is determined by a sulphated and acylated glucosamine oligosaccharide signalNature, 1990
- Fatty acylation of proteinsBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1989
- Proton Motive Force Involved in Protein Transport Across the Outer Membrane of Aeromonas salmonicidaScience, 1989
- Transcription antitermination in an Escherichia coli haemolysin operon is directed progressively by cis‐acting DNA sequences upstream of the promoter regionMolecular Microbiology, 1989
- Multiple Mechanisms of Protein Insertion into and Across MembranesScience, 1985