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Improved secretion of glycoproteins using an N-glycan-restricted passport sequence tag recognized by cargo receptor

Author

Listed:
  • Hirokazu Yagi

    (Nagoya City University)

  • Maho Yagi-Utsumi

    (Nagoya City University
    National Institutes of Natural Sciences
    National Institutes of Natural Sciences
    SOKENDAI (The Graduate University for Advanced Studies))

  • Rena Honda

    (Nagoya City University
    National Institutes of Natural Sciences
    SOKENDAI (The Graduate University for Advanced Studies))

  • Yusaku Ohta

    (National Institutes of Natural Sciences
    National Institutes of Natural Sciences)

  • Taiki Saito

    (Nagoya City University)

  • Miho Nishio

    (Nagoya City University)

  • Satoshi Ninagawa

    (National Institutes of Natural Sciences)

  • Kousuke Suzuki

    (Nagoya City University)

  • Takahiro Anzai

    (National Institutes of Natural Sciences)

  • Yukiko Kamiya

    (National Institutes of Natural Sciences)

  • Kazuhiro Aoki

    (National Institutes of Natural Sciences
    National Institutes of Natural Sciences)

  • Mahito Nakanishi

    (National Institute of Advanced Industrial Science and Technology (AIST))

  • Tadashi Satoh

    (Nagoya City University)

  • Koichi Kato

    (Nagoya City University
    National Institutes of Natural Sciences
    National Institutes of Natural Sciences
    SOKENDAI (The Graduate University for Advanced Studies))

Abstract

MCFD2 and ERGIC-53, which are the products of causative genes of combined factor V and factor VIII deficiency, form a cargo receptor complex responsible for intracellular transport of these coagulation factors in the early secretory pathway. In this study, using an NMR technique, we successfully identified an MCFD2-binding segment from factor VIII composed of a 10 amino acid sequence that enhances its secretion. This prompted us to examine possible effects of attaching this sequence to recombinant glycoproteins on their secretion. We found that the secretion level of recombinant erythropoietin was significantly increased simply by tagging it with the passport sequence. Our findings not only provide molecular basis for the intracellular trafficking of coagulation factors and their genetic deficiency but also offer a potentially useful tool for increasing the production yields of recombinant glycoproteins of biopharmaceutical interest.

Suggested Citation

  • Hirokazu Yagi & Maho Yagi-Utsumi & Rena Honda & Yusaku Ohta & Taiki Saito & Miho Nishio & Satoshi Ninagawa & Kousuke Suzuki & Takahiro Anzai & Yukiko Kamiya & Kazuhiro Aoki & Mahito Nakanishi & Tadash, 2020. "Improved secretion of glycoproteins using an N-glycan-restricted passport sequence tag recognized by cargo receptor," Nature Communications, Nature, vol. 11(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-15192-1
    DOI: 10.1038/s41467-020-15192-1
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    Cited by:

    1. Satoshi Watanabe & Yoshiaki Kise & Kento Yonezawa & Mariko Inoue & Nobutaka Shimizu & Osamu Nureki & Kenji Inaba, 2024. "Structure of full-length ERGIC-53 in complex with MCFD2 for cargo transport," Nature Communications, Nature, vol. 15(1), pages 1-13, December.

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