Molecular characterization of an exceptionally acidic lysozyme-like protein from the protozoon Entamoeba histolytica.
The protozoan parasite Entamoeba histolytica contains a second antibacterial protein with lysozyme-like properties. The newly recognized bacteriolytic protein was purified from extracts of amoebic trophozoites to allow amino-terminal sequencing. Subsequent molecular cloning revealed that it is an isoform of the amoeba lysozyme described previously but also demonstrated a substantial sequence divergence of the two forms. As lysozymes typically are basic proteins, the novel amoebic protein differs markedly in having a pI of 4.5. There is no significant similarity of both amoeba lysozymes with any bacteriolytic protein of other organisms reported so far; however, striking sequence identity is found with predicted gene products of unknown function derived from the bacteria-feeding nematode Caenorhabditis elegans.
Nickel
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R
Bernhard Nocht Institute for Tropical Medicine, Hamburg, Germany.
Jacobs
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T
Leippe
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M
D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D015139:Blotting, Southern; D017173:Caenorhabditis elegans / Q000737:chemistry; D003001:Cloning, Molecular; D004748:Entamoeba histolytica / Q000737:chemistry*; D008969:Molecular Sequence Data; D009113:Muramidase / Q000737:chemistry* / Q000235:genetics; D017386:Sequence Homology, Amino Acid
D009113:Muramidase