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Hydrophobin (HFBI): A potential fusion partner for one-step purification of recombinant proteins from insect cells

机译：疏水蛋白（HFBI）：从昆虫细胞一步纯化重组蛋白的潜在融合伙伴

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摘要

Hydrophobins play an important role in binding and assembly of fungal surface structures as well as in medium-air interactions. These, hydrophobic properties provide interesting possibilities when purification of macromolecules is concerned. In aqueous micellar two-phase systems, based on surfactants, the water soluble hydrophobins are concentrated inside micellar structures and, thus, distributed to defined aqueous phases. This, one-step purification is attractive particularly when large-scale production of recombinant proteins is concerned. In the present study the hydrophobin HFBI of Trichoderma reesei was expressed as an N-terminal fusion with chicken avidin in baculovirus infected insect cells. The intracellular distribution of the recombinant fusion construct was analyzed by confocal microscopy and the protein subsequently purified from cytoplasmic extracts in an aqueous micellar two-phase system by using a non-ionic surfactant. The results show that hydrophobin and an avidin fusion thereof were efficiently expressed in insect cells and that these hydrophobic proteins could be efficiently purified from these cells in one-step by adopting an aqueous micellar two-phase system. (C) 2008 Elsevier Inc. All rights reserved.
机译：疏水蛋白在真菌表面结构的结合和组装以及空气与空气的相互作用中起着重要作用。当涉及大分子纯化时，这些疏水性质提供了有趣的可能性。在基于表面活性剂的胶束水两相系统中，水溶性疏水蛋白浓缩在胶束结构内部，因此分布在确定的水相中。这种一步纯化法特别有吸引力，尤其是在大规模生产重组蛋白时。在本研究中，里氏木霉的疏水蛋白HFBI被表达为与杆状病毒感染的昆虫细胞中的鸡抗生物素蛋白的N末端融合体。通过共聚焦显微镜分析重组融合构建体的胞内分布，随后通过使用非离子表面活性剂在水性胶束两相系统中从细胞质提取物中纯化蛋白质。结果表明疏水蛋白及其抗生物素蛋白融合体在昆虫细胞中有效表达，并且通过采用水性胶束两相系统可以一步一步地从这些细胞中有效地纯化这些疏水蛋白。 （C）2008 Elsevier Inc.保留所有权利。

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