Recombinant jacalin-like plant lectins are produced at high levels in Nicotiana benthamiana and retain agglutination activity and sugar specificity
Recombinant jacalin-like plant lectins are produced at high levels in Nicotiana benthamiana and retain agglutination activity and sugar specificity
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DOI：
10.1016/j.jbiotec.2012.11.017
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发表时间：
2013-02-20
影响因子：
4.1
通讯作者：
Orzaez, Diego
中科院分区：
文献类型：
--
作者：
Fernandez-del-Carmen, Asun;Juarez, Paloma;Orzaez, Diego
植物界是一个未充分开发的有价值的蛋白质来源，像植物凝集素，显示独特的相互作用的特异性。此外，植物蛋白多样性由于天然来源的低可用性和异质性而仍未得到充分利用。所有这些障碍都可以通过重组生产来克服。天然来源和重组平台之间的狭窄系统发育差距可能有助于适当的蛋白质加工和稳定性;因此，植物细胞底盘应特别适合于许多植物天然蛋白质的重组生产。这在本文中通过使用最先进的magnICON技术在本氏烟草（Nicotiana benthamiana）中重组产生植物jacalin相关凝集素（JRL）蛋白家族的两种代表来说明。甘露糖特异性Banlec JRL在叶中以非常高的水平产生，达到每克鲜重1.0毫克的纯化蛋白，并显示出强的凝集活性。半乳糖专一性的jacalin JRL，其复杂的加工要求，也成功地在N。每克鲜重0.25毫克纯化蛋白质的水平。重组Jacalin（rJacalin）被证明是有效的人IgA 1的纯化，并能够区分植物和天然IgA 1，由于其差异的糖基化状态。总之，这些结果表明，植物细胞工厂应被认为是重组生产有价值的植物蛋白的主要选择。(C)2012 Elsevier B. V.保留所有权利。
The plant kingdom is an underexplored source of valuable proteins which, like plant lectins, display unique interacting specificities. Furthermore, plant protein diversity remains under-exploited due to the low availability and heterogeneity of native sources. All these hurdles could be overcome with recombinant production. A narrow phylogenetic gap between the native source and the recombinant platform is likely to facilitate proper protein processing and stability; therefore, the plant cell chassis should be specially suited for the recombinant production of many plant native proteins. This is illustrated herein with the recombinant production of two representatives of the plant jacalin-related lectin (JRLs) protein family in Nicotiana benthamiana using state-of-the-art magnICON technology. Mannose-specific Banlec JRL was produced at very high levels in leaves, reaching 1.0 mg of purified protein per gram of fresh weight and showing strong agglutination activity. Galactose-specific jacalin JRL, with its complicated processing requirements, was also successfully produced in N. benthamiana at levels of 0.25 mg of purified protein per gram of fresh weight. Recombinant Jacalin (rJacalin) proved efficient in the purification of human IgA1, and was able to discriminate between plant-made and native IgA1 due to their differential glycosylation status. Together, these results show that the plant cell factory should be considered a primary option in the recombinant production of valuable plant proteins. (C) 2012 Elsevier B.V. All rights reserved.