Molecular characterization of an exceptionally acidic lysozyme-like protein from the protozoan Entamoeba histolytica

被引:17
作者
Nickel, R [1 ]
Jacobs, T [1 ]
Leippe, M [1 ]
机构
[1] Bernhard Nocht Inst Trop Med, D-20359 Hamburg, Germany
来源
FEBS LETTERS | 1998年 / 437卷 / 1-2期
关键词
acidic lysozyme; antibacterial protein; N-acetylmuramidase; protozoon; Entamoeba histolytica;
D O I
10.1016/S0014-5793(98)01220-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 1998 Federation of European Biochemical Societies.
引用
收藏
页码:153 / 157
页数:5
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