Pore-forming peptides of Entamoeba dispar : similarity and divergence to amoebapores in structure, expression and activity

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Item Type:	Article
Title:	Pore-forming peptides of Entamoeba dispar : similarity and divergence to amoebapores in structure, expression and activity
Creators Name:	Nickel, R., Ott, C., Dandekar, T. and Leippe, M.
Abstract:	Amoebapore, a 77-residue peptide with pore-forming activity from the human pathogen Entamoeba histolytica, is implicated in the killing of phagocytosed bacteria and in the cytolytic reaction of the amoeba against host cells. Previously, we structurally and functionally characterized three amoebapore isoforms in E. histolytica but recognized only one homolog in the closely related but non-pathogenic species Entamoeba dispar. Here, we identified two novel amoebapore homologs from E. dispar by molecular cloning. Despite strong resemblance of the primary structures of the homologs, molecular modeling predicts a species-specific variance between the peptide structures. Parallel isolation from trophozoite extracts of the two species revealed a lower amount of pore-forming peptides in E. dispar and substantially higher activity of the major isoform from E. histolytica towards natural membranes than that from E. dispar. Differences in abundance and activity of the lytic polypeptides may have an impact on the pathogenicity of amoebae.
Keywords:	Amoebapore, Antibacterial Peptide, Entamoeba, Pore Formation, Saposin-Like Proteins, Animals
Source:	European Journal of Biochemistry
ISSN:	0014-2956
Publisher:	Blackwell Publishing
Volume:	265
Number:	3
Page Range:	1002-1007
Date:	1 November 1999
Official Publication:	https://doi.org/10.1046/j.1432-1327.1999.00807.x
PubMed:	View item in PubMed

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