Van Damme E J, Barre A, Rougé P, Van Leuven F, Peumans W J
Laboratory for Phytopathology and Plant Protection, Katholieke Universiteit Leuven, Belgium.
Eur J Biochem. 1996 Jan 15;235(1-2):128-37. doi: 10.1111/j.1432-1033.1996.00128.x.
The cDNA encoding the NeuAc(alpha-2,6)Gal/GalNAc binding lectin from elderberry (Sambucus nigra) bark (SNAI) was isolated from a cDNA library constructed with mRNA from the bark. Sequence analysis of this lectin cDNA revealed a striking similarity to the previously sequenced type-2 ribosome-inactivating proteins from Ricinus communis and Abrus precatorius. Molecular modelling of SNAI further indicated that its structure closely resembles that of ricin. Since SNAI strongly inhibits cell-free protein synthesis in a rabbit reticulocyte lysate it presumably is a type-2 ribosome-inactivating protein. However, SNAI differs from all previously described type-2 ribosome-inactivating proteins by its specificity towards NeuAc(alpha-2,6)Gal/GalNAc and its unusual molecular structure.
从接骨木(黑接骨木)树皮构建的cDNA文库中分离出编码NeuAc(α-2,6)Gal/GalNAc结合凝集素(SNAI)的cDNA。对该凝集素cDNA的序列分析显示,它与蓖麻和相思豆中先前测序的2型核糖体失活蛋白有显著相似性。SNAI的分子建模进一步表明,其结构与蓖麻毒素的结构非常相似。由于SNAI强烈抑制兔网织红细胞裂解物中的无细胞蛋白质合成,推测它是一种2型核糖体失活蛋白。然而,SNAI与所有先前描述的2型核糖体失活蛋白的不同之处在于其对NeuAc(α-2,6)Gal/GalNAc的特异性及其不寻常的分子结构。