IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v13y2022i1d10.1038_s41467-022-34128-5.html
   My bibliography  Save this article

Ectopic expression of sericin enables efficient production of ancient silk with structural changes in silkworm

Author

Listed:
  • Xuedong Chen

    (Suzhou Medical College, Soochow University
    Soochow University)

  • Yongfeng Wang

    (Suzhou Medical College, Soochow University
    Soochow University)

  • Yujun Wang

    (Beibu Gulf University)

  • Qiuying Li

    (Suzhou Medical College, Soochow University
    Soochow University)

  • Xinyin Liang

    (Suzhou Medical College, Soochow University
    Soochow University)

  • Guang Wang

    (Suzhou Medical College, Soochow University
    Soochow University)

  • Jianglan Li

    (Suzhou Medical College, Soochow University
    Soochow University)

  • Ruji Peng

    (Suzhou Medical College, Soochow University
    Soochow University)

  • Yanghu Sima

    (Suzhou Medical College, Soochow University
    Soochow University)

  • Shiqing Xu

    (Suzhou Medical College, Soochow University
    Soochow University)

Abstract

Bombyx mori silk is a super-long natural protein fiber with a unique structure and excellent performance. Innovative silk structures with high performance are in great demand, thus resulting in an industrial bottleneck. Herein, the outer layer sericin SER3 is ectopically expressed in the posterior silk gland (PSG) in silkworms via a piggyBac-mediated transgenic approach, then secreted into the inner fibroin layer, thus generating a fiber with sericin microsomes dispersed in fibroin fibrils. The water-soluble SER3 protein secreted by PSG causes P25’s detachment from the fibroin unit of the Fib-H/Fib-L/P25 polymer, and accumulation between the fibroin layer and the sericin layer. Consequently, the water solubility and stability of the fibroin-colloid in the silk glandular cavity, and the crystallinity increase, and the mechanical properties of cocoon fibers, moisture absorption and moisture liberation of the silk also improve. Meanwhile, the mutant overcomes the problems of low survival and abnormal silk gland development, thus enabling higher production efficiency of cocoon silk. In summary, we describe a silk gland transgenic target protein selection strategy to alter the silk fiber structure and to innovate its properties. This work provides an efficient and green method to produce silk fibers with new functions.

Suggested Citation

  • Xuedong Chen & Yongfeng Wang & Yujun Wang & Qiuying Li & Xinyin Liang & Guang Wang & Jianglan Li & Ruji Peng & Yanghu Sima & Shiqing Xu, 2022. "Ectopic expression of sericin enables efficient production of ancient silk with structural changes in silkworm," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
  • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-34128-5
    DOI: 10.1038/s41467-022-34128-5
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-022-34128-5
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/s41467-022-34128-5?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    References listed on IDEAS

    as
    1. Hyoung-Joon Jin & David L. Kaplan, 2003. "Mechanism of silk processing in insects and spiders," Nature, Nature, vol. 424(6952), pages 1057-1061, August.
    Full references (including those not matched with items on IDEAS)

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    1. D. Eliaz & S. Paul & D. Benyamin & A. Cernescu & S. R. Cohen & I. Rosenhek-Goldian & O. Brookstein & M. E. Miali & A. Solomonov & M. Greenblatt & Y. Levy & U. Raviv & A. Barth & U. Shimanovich, 2022. "Micro and nano-scale compartments guide the structural transition of silk protein monomers into silk fibers," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    2. Jianming Chen & Arata Tsuchida & Ali D. Malay & Kousuke Tsuchiya & Hiroyasu Masunaga & Yui Tsuji & Mako Kuzumoto & Kenji Urayama & Hirofumi Shintaku & Keiji Numata, 2024. "Replicating shear-mediated self-assembly of spider silk through microfluidics," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    3. Ke Wang & Qian Ma & Xiao Qin & Shu Dong Wang, 2018. "Silk Fibroin and its Application in Tissue Engineering," Current Trends in Fashion Technology & Textile Engineering, Juniper Publishers Inc., vol. 4(4), pages 74-76, November.
    4. Wenbo Hu & Anqiang Jia & Sanyuan Ma & Guoqing Zhang & Zhaoyuan Wei & Fang Lu & Yongjiang Luo & Zhisheng Zhang & Jiahe Sun & Tianfang Yang & TingTing Xia & Qinhui Li & Ting Yao & Jiangyu Zheng & Zijie , 2023. "A molecular atlas reveals the tri-sectional spinning mechanism of spider dragline silk," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    5. Chenchen Wu & Yu Duan & Lintao Yu & Yao Hu & Chenxi Zhao & Chunwang Ji & Xiangdong Guo & Shu Zhang & Xiaokang Dai & Puyi Ma & Qian Wang & Shengjie Ling & Xiaoxia Yang & Qing Dai, 2024. "In-situ observation of silk nanofibril assembly via graphene plasmonic infrared sensor," Nature Communications, Nature, vol. 15(1), pages 1-9, December.
    6. Tina Arndt & Kristaps Jaudzems & Olga Shilkova & Juanita Francis & Mathias Johansson & Peter R. Laity & Cagla Sahin & Urmimala Chatterjee & Nina Kronqvist & Edgar Barajas-Ledesma & Rakesh Kumar & Gefe, 2022. "Spidroin N-terminal domain forms amyloid-like fibril based hydrogels and provides a protein immobilization platform," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    7. Ori Brookstein & Eyal Shimoni & Dror Eliaz & Ifat Kaplan-Ashiri & Itay Carmel & Ulyana Shimanovich, 2024. "Metal ions guide the production of silkworm silk fibers," Nature Communications, Nature, vol. 15(1), pages 1-13, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-34128-5. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.