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. 1992 Oct;11(10):3501–3506. doi: 10.1002/j.1460-2075.1992.tb05432.x

Primary and secondary structure of the pore-forming peptide of pathogenic Entamoeba histolytica.

M Leippe 1, E Tannich 1, R Nickel 1, G van der Goot 1, F Pattus 1, R D Horstmann 1, H J Müller-Eberhard 1
PMCID: PMC556807  PMID: 1396552

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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Selected References

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