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Pore‐forming peptides of Entamoeba dispar : Similarity and divergence to amoebapores in structure, expression and activity by Rosa Nickel; Claudia Ott; Thomas Dandekar; Matthias Leippe is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Pore‐forming peptides of Entamoeba dispar : Similarity and divergence to amoebapores in structure, expression and activity about?

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.

Who reads Pore‐forming peptides of Entamoeba dispar : Similarity and divergence to amoebapores in structure, expression and activity?

Author

Rosa Nickel; Claudia Ott; Thomas Dandekar; Matthias Leippe

Publisher

John Wiley and Sons; Springer; Wiley (Blackwell Publishing); Springer-Verlag; Blackwell Publishing Inc.; Springer Verlag; Wiley; Springer Science and Business Media LLC (ISSN 1432-1327)

Published

1999

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)