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Molecular characterization of an exceptionally acidic lysozyme‐like protein from the protozoon Entamoeba histolytica
Author(s) -
Nickel Rosa,
Jacobs Thomas,
Leippe Matthias
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01220-4
Subject(s) - lysozyme , entamoeba histolytica , biology , peptide sequence , entamoeba , microbiology and biotechnology , biochemistry , muramidase , gene
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 p I 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 .