ArticleThe EMBO journal1992
Primary and secondary structure of the pore-forming peptide of pathogenic Entamoeba histolytica.
Article in The EMBO journal, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Synthetic bovine NK-lysin-derived peptide (bNK2A) does not require intra-chain disulfide bonds for bactericidal activity.PloS one · 2019Article
- Comparative Transcriptomic Exploration Reveals Unique Molecular Adaptations of Neuropathogenic Trichobilharzia to Invade and Parasitize Its Avian Definitive Host.PLoS neglected tropical diseases · 2016Article
- Intestinal invasion by Entamoeba histolytica.Sub-cellular biochemistry · 2008Article
- The second cysteine protease inhibitor, EhICP2, has a different localization in trophozoites of Entamoeba histolytica than EhICP1.Parasitology research · 2006Article
- Amoebapores and NK-lysin, members of a class of structurally distinct antimicrobial and cytolytic peptides from protozoa and mammals: a comparative functional analysis.The Biochemical journal · 2003Article
- Laboratory diagnosis of amebiasis.Clinical microbiology reviews · 2003Review
- Intermediate subunit of the Gal/GalNAc lectin of Entamoeba histolytica is a member of a gene family containing multiple CXXC sequence motifs.Infection and immunity · 2001Article
- Bacteriocin AS-48, a microbial cyclic polypeptide structurally and functionally related to mammalian NK-lysin.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Pathogenesis of intestinal amebiasis: from molecules to disease.Clinical microbiology reviews · 2000Review
- Down regulation of Entamoeba histolytica virulence by monoxenic cultivation with Escherichia coli O55 is related to a decrease in expression of the light (35-kilodalton) subunit of the Gal/GalNAc lectin.Infection and immunity · 1999Article
- Hsp60 is targeted to a cryptic mitochondrion-derived organelle ("crypton") in the microaerophilic protozoan parasite Entamoeba histolytica.Molecular and cellular biology · 1999Article
- Saposins and their interaction with lipids.Neurochemical research · 1999Review
- Molecular and functional characterization of a recombinant protein of Trichuris trichiura.Proceedings. Biological sciences · 1998Article
- A new gene family (ariel) encodes asparagine-rich Entamoeba histolytica antigens, which resemble the amebic vaccine candidate serine-rich E. histolytica protein.Infection and immunity · 1998Article
- Contact-dependent transfer of the galactose-specific lectin of Entamoeba histolytica to the lateral surface of enterocytes in culture.Infection and immunity · 1995Article
- Modification of membrane permeability by animal viruses.Advances in virus research · 1995Review
- Adherence and cytotoxicity of Entamoeba histolytica or how lectins let parasites stick around.Infection and immunity · 1994Review
- Cytolytic and antibacterial activity of synthetic peptides derived from amoebapore, the pore-forming peptide of Entamoeba histolytica.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- Acid sphingomyelinase possesses a domain homologous to its activator proteins: saposins B and D.Protein science : a publication of the Protein Society · 1994Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A pore-forming peptide is implicated in the potent cytolytic activity of pathogenic Entamoeba histolytica. Using NH2-terminal sequence information of this peptide, the corresponding cDNA was isolated. The cDNA-deduced amino acid sequence revealed a putative signal peptide and a mature peptide of 77 amino acids including six cysteine residues. Computer-aided secondary structure analysis predicted that the peptide would be composed of four adjacent alpha-helices, and CD spectroscopy indicated an all alpha-helical conformation. The tertiary structure appears to be stabilized by three disulfide bonds; the pore-forming activity was not sensitive to heat but was lost in the presence of reducing agents. Sequence homology was found to the saposins and to surfactant-associated protein B, both mammalian polypeptides of similar size and secondary structure but of non-lytic function. In particular, the six cysteine residues were found to be conserved, suggesting a common motif for stabilizing a favourable tertiary structure. Compared with previously characterized toxic peptides also containing three disulfide bonds, the amoeba peptide may represent a distinct class of biologically active peptides.
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