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An Embeddable Molecular Code for Lewis X Modification Through Interaction with Fucosyltansferase 9
Open accessPreprint — published as 10.1038/s42003-022-03616-1
Abstract
N-glycans are diversified by a panel of glycosyltransferases in the Golgi, which are supposed to modify various glycoproteins in promiscuous manners, resulting in unpredictable glycosylation profiles in general. In contrast, our previous study showed that fucosyltransferase 9 (FUT9) generates Lewis X glycotopes primarily on lysosome-associated membrane protein 1 (LAMP-1) in neural stem cells. Here, we demonstrate that a contiguous 29-amino acid sequence in the N-terminal domain of LAMP-1 is indispensable for FUT9-dependent Lewis X modification. Interestingly, Lewis X modification was induced on erythropoietin as a model glycoprotein both in vivo and in vitro, just by attaching this sequence to its C-terminus. Based on these results, we conclude that the amino acid sequence from LAMP-1 functions as a “Lewis X code”, which is deciphered by FUT9, and can be embedded into other glycoproteins to evoke a Lewis X modification, opening up new possibilities for protein engineering and cell engineering.
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Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
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Metadata
- Authors
- Saito, T., Yagi, H., Kuo, C.-W., Khoo, K.-H., & Kato, K.
- Affiliations
- National Institutes of Natural Sciences (JP)
- Institute of Biological Chemistry, Academia Sinica (TW)
- Corresponding author
- Kato, Koichi
- Venue
- Communications Biology
- Published
- 2021-12-28
- Volume
- 5
- Issue
- 1
- Pages
- 676-676
- ISSN
- 2399-3642 (ISSN-L)
- PMC
- PMC9279290
- OpenAlex
- W4285393251
- Cited by
- 9
- References
- 1
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 3 · 2022: 1
- FWCI
- 0.49
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Communications Biology (publishedVersion, cc-by)
- Research Square (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Academia Sinica (AS-CFII-108-10 7, AS-IA-105-L02)
- Nagoya City University
- Japan Society for the Promotion of Science (JP17H06414, JP25102008, JP21H02625, 23K21358, CREST, 24249002, 20K21495, 20J23703)
- Core Research for Evolutional Science and Technology (JPMJCR21E3)
- Exploratory Research Center on Life and Living Systems, National Institutes of Natural Sciences (22EXC304, 21-302)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
- Keywords
- CD15, LAMP1, N-glycosylation, glycosyltransferase substrate specificity, glycoprotein modification, erythropoietin, protein engineering, cell engineering, Golgi glycosylation
- MeSH terms
- Fucosyltransferases, Glycoproteins, Glycosylation, Polysaccharides, Lewis X Antigen
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