Nickel R, Jacobs T, Leippe M
Bernhard Nocht Institute for Tropical Medicine, Hamburg, Germany.
FEBS Lett. 1998 Oct 16;437(1-2):153-7. doi: 10.1016/s0014-5793(98)01220-4.
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.
原生动物寄生虫溶组织内阿米巴含有第二种具有溶菌酶样特性的抗菌蛋白。从阿米巴滋养体提取物中纯化出这种新发现的溶菌蛋白，以便进行氨基末端测序。随后的分子克隆表明，它是先前描述的阿米巴溶菌酶的一种同工型，但也显示出这两种形式在序列上有很大差异。由于溶菌酶通常是碱性蛋白，这种新型阿米巴蛋白的显著不同之处在于其pI为4.5。到目前为止，这两种阿米巴溶菌酶与其他生物的任何溶菌蛋白都没有明显的相似性；然而，与取食细菌的线虫秀丽隐杆线虫来源的功能未知的预测基因产物有显著的序列同一性。
