Purification and Functional Characterization of the Effects on Cell Signaling of Mytilectin: A Novel β-Trefoil Lectin from Marine Mussels
Purification and Functional Characterization of the Effects on Cell Signaling of Mytilectin: A Novel β-Trefoil Lectin from Marine Mussels
复制标题
贻贝凝集素对细胞信号转导影响的纯化和功能表征：来自海洋贻贝的新型 β-三叶凝集素
DOI：
10.1007/978-1-0716-0430-4_21
复制
发表时间：
2020
影响因子：
--
通讯作者：
Ozeki Yasuhiro
中科院分区：
文献类型：
--
作者：
Fujii Yuki;Kawsar S. M. Abe;Hasan Imtiaj;Fujita Hideaki;Gerdol Marco;Ozeki Yasuhiro
在2010年代，已经在贻贝科（软体动物门）的海洋贻贝中鉴定出具有β-三叶折叠的新型凝集素家族。“MytiLec-1”，在本章中描述的凝集素，是这个家庭的第一个成员被分离和地中海musselMytilus galloprovincialis，一个商业和生态上重要的物种，分布在世界各地的海洋沿海地区的特点。MytiLec-1与α-半乳糖苷球三糖（Gb 3：Galα1-4Galβ1-4Glc）的糖部分结合，导致表达Gb 3的伯基特淋巴瘤细胞凋亡。虽然MytiLec-1的一级结构非常不寻常，但其三维结构排列为β-三叶折叠，这是在广泛的生物体中发现的“蓖麻毒素B链（或R）型”凝集素的典型结构。迄今为止，MytiLec-1样凝集素仅存在于软体动物科的少数物种中（M. galloprovincialis，M. trossulus，M. californianus和Crenomytilus grayanus）和腕足动物门。转录组数据显示贻贝中存在不同结构形式的mytilectin，其中包括原型和嵌合型蛋白。这些凝集素的一级序列与任何先前描述的已知蛋白质家族不匹配，导致它们被分配到新的“mytilectin家族”。我们在这里报告的纯化方法，这种凝集素，并描述其在细胞生物学中的应用。
In the 2010s, a novel lectin family with β-trefoil folding has been identified in marine mussels from the family Mytilidae (phylum Mollusca). “MytiLec-1,” the lectin described in this chapter, was the first member of this family to be isolated and characterized from the Mediterranean musselMytilus galloprovincialis, a commercially and ecologically important species, spread in marine coastal areas worldwide. MytiLec-1 bound to the sugar moiety of globotriose (Gb3: Galα1-4Galβ1-4Glc), an α-galactoside, leading to apoptosis of Gb3-expressing Burkitt’s lymphoma cells. Although the primary structure of MytiLec-1 was quite unusual, its three-dimensional structure was arranged as a β-trefoil fold, which is the typical architecture of “Ricin B chain (or R)-type” lectins, which are found in a broad range of organisms. To date, MytiLec-1-like lectins have been exclusively found in a few species of the mollusk family Mytilidae (M. galloprovincialis,M. trossulus, M. californianus, andCrenomytilus grayanus) and in the phylum Brachiopoda. Transcriptome data revealed the presence of different structural forms of mytilectin in mussels, which included prototype and chimera-type proteins. The primary sequence of these lectins did not match any previously described known protein family, leading to their assignment to the new “mytilectin family.” We here report the method of purification of this lectin and describe its use in cell biology.