Neosilk Laboratory, Immuno-Biological Laboratories, Co., Ltd., Higashihiroshima, Hiroshima, Japan.
Biotechnol Lett. 2011 Apr;33(4):645-54. doi: 10.1007/s10529-010-0498-z. Epub 2010 Dec 24.
As a result of breeding for more than 4,000 years, the silkworm, Bombyx mori, has acquired the ability to synthesize bulk amounts of silk proteins in its silk glands. To utilize this capacity for mass production of useful proteins, transgenic silkworms were generated that synthesized recombinant proteins in the silk gland and secreted them into the silk cocoon. The silk gland is classified into two main regions: the posterior (PSG) and the middle silk gland (MSG). By controlling the expressed regions of the recombinant protein gene in the silk gland, we were able to control the localization of the synthesized protein in the silk thread. Expression in the PSG or MSG led to localization in the insoluble fibroin core or hydrophilic outer sericin layer, respectively. This review focuses on the expression of recombinant protein in the MSG of transgenic silkworms. The recombinant protein secreted in the sericin layer is extractable from the cocoon with only a small amount of endogenous silk protein contamination by soaking the cocoon in mild aqueous solutions. The possibility of utilizing transgenic silkworms as a valuable tool for the mass production of therapeutic and industrially relevant recombinant proteins is discussed.
经过 4000 多年的培育，家蚕已经获得了在丝腺中大量合成丝蛋白的能力。为了利用这种能力大规模生产有用的蛋白质，我们生成了转基因家蚕，使其在丝腺中合成重组蛋白并将其分泌到丝茧中。丝腺分为两个主要区域：后部丝腺（PSG）和中部丝腺（MSG）。通过控制丝腺中重组蛋白基因的表达区域，我们能够控制合成蛋白在丝线中的定位。在 PSG 或 MSG 中的表达分别导致定位在不溶性丝素核心或亲水性外层丝胶层中。这篇综述重点介绍了在转基因家蚕的 MSG 中表达重组蛋白的情况。在丝胶层中分泌的重组蛋白可以通过将茧浸泡在温和的水溶液中，从茧中提取出来，而仅少量内源性丝蛋白受到污染。讨论了利用转基因家蚕作为大规模生产治疗性和工业相关重组蛋白的有价值工具的可能性。
