Van Damme E J, Balzarini J, Smeets K, Van Leuven F, Peumans W J
Laboratory for Phytopathology and Plant Protection, Katholieke Universiteit Leuven, Belgium.
Glycoconj J. 1994 Aug;11(4):321-32. doi: 10.1007/BF00731205.
The Orchidaceae species Listera ovata and Epipactis helleborine contain two types of mannose-binding proteins. Using a combination of affinity chromatography on mannose-Sepharose-4B and ion exchange chromatography on a Mono-S column eight different mannose-binding proteins were isolated from the leaves of Listera ovata. Whereas seven of these mannose-binding proteins have agglutination activity and occur as dimers composed of lectin subunits of 11-13 kDa, the eighth mannose-binding protein is a monomer of 14 kDa devoid of agglutination activity. Moreover, the monomeric mannose-binding protein does not react with an antiserum raised against the dimeric lectin and, in contrast to the lectins, is completely inactive when tested for antiretroviral activity against human immunodeficiency virus type 1 and type 2. Mannose-binding proteins with similar properties were also found in the leaves of Epipactis helleborine. However, in contrast to Listera only one lectin was found in Epipactis. Despite the obvious differences in molecular structure and biological activities molecular cloning of different mannose-binding proteins from Listera and Epipactis has shown that these proteins are related and some parts of the sequences show a high degree of sequence homology indicating that they have been conserved through evolution.
兰科植物卵叶对叶兰和欧洲火烧兰含有两种类型的甘露糖结合蛋白。通过结合使用甘露糖 - 琼脂糖 - 4B亲和层析和Mono - S柱离子交换层析，从卵叶对叶兰的叶子中分离出了八种不同的甘露糖结合蛋白。其中七种甘露糖结合蛋白具有凝集活性，以由11 - 13 kDa凝集素亚基组成的二聚体形式存在，而第八种甘露糖结合蛋白是一种14 kDa的单体，没有凝集活性。此外，单体甘露糖结合蛋白不与针对二聚体凝集素产生的抗血清发生反应，并且与凝集素不同，在针对人类免疫缺陷病毒1型和2型的抗逆转录病毒活性测试中完全无活性。在欧洲火烧兰的叶子中也发现了具有类似性质的甘露糖结合蛋白。然而，与卵叶对叶兰不同，在欧洲火烧兰中仅发现一种凝集素。尽管在分子结构和生物学活性上存在明显差异，但对卵叶对叶兰和欧洲火烧兰中不同甘露糖结合蛋白的分子克隆表明，这些蛋白是相关的，并且序列的某些部分显示出高度的序列同源性，表明它们在进化过程中得以保留。
