Kato Kentaro, Yahata Kazuhide, Gopal Dhoubhadel Bhim, Fujii Yoshito, Tachibana Hiroshi
Department of Parasitology Institute of Tropical Medicine (NEKKEN), Nagasaki University, 1-12-4 Sakamoto, Nagasaki, 852-8523, Japan.
Department of Protozoology Institute of Tropical Medicine (NEKKEN), Nagasaki University, 1-12-4 Sakamoto, Nagasaki, 852-8523, Japan.
Sci Rep. 2015 Sep 10;5:13901. doi: 10.1038/srep13901.
Galactose and N-acetyl-D-galactosamine (Gal/GalNAc) inhibitable lectin of Entamoeba histolytica, a common protozoan parasite, has roles in pathogenicity and induction of protective immunity in mouse models of amoebiasis. The lectin consists of heavy (Hgl), light (Lgl), and intermediate (Igl) subunits. Hgl has lectin activity and Lgl does not, but little is known about the activity of Igl. In this study, we assessed various regions of Igl for hemagglutinating activity using recombinant proteins expressed in Escherichia coli. We identified a weak hemagglutinating activity of the protein. Furthermore, we found novel hemolytic and cytotoxic activities of the lectin, which resided in the carboxy-terminal region of the protein. Antibodies against Igl inhibited the hemolytic activity of Entamoeba histolytica trophozoites. This is the first report showing hemagglutinating, hemolytic and cytotoxic activities of an amoebic molecule, Igl.
溶组织内阿米巴是一种常见的原生动物寄生虫,其半乳糖和N-乙酰-D-半乳糖胺(Gal/GalNAc)抑制性凝集素在阿米巴病小鼠模型的致病性和保护性免疫诱导中发挥作用。该凝集素由重链(Hgl)、轻链(Lgl)和中间链(Igl)亚基组成。Hgl具有凝集素活性,而Lgl没有,但关于Igl的活性知之甚少。在本研究中,我们使用在大肠杆菌中表达的重组蛋白评估了Igl的各个区域的血凝活性。我们鉴定出该蛋白具有微弱的血凝活性。此外,我们发现该凝集素具有新的溶血和细胞毒性活性,这些活性存在于该蛋白的羧基末端区域。针对Igl的抗体抑制了溶组织内阿米巴滋养体的溶血活性。这是首次报道显示阿米巴分子Igl具有血凝、溶血和细胞毒性活性。