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An embeddable molecular code for Lewis X modification through interaction with fucosyltransferase 9.

Taiki Saito1,2, Hirokazu Yagi1,3, Chu-Wei Kuo4

  • 1Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya, 467-8603, Japan.

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A specific 29-amino acid sequence in lysosome-associated membrane protein 1 (LAMP-1) acts as a "Lewis X code." This code directs fucosyltransferase 9 (FUT9) to add Lewis X structures to proteins, enabling new protein engineering applications.

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Area of Science:

  • Glycobiology
  • Protein Engineering
  • Cellular Biology

Background:

  • N-glycan diversification by glycosyltransferases typically results in unpredictable glycosylation profiles.
  • Previous research identified fucosyltransferase 9 (FUT9) as a key enzyme for Lewis X glycotopes on lysosome-associated membrane protein 1 (LAMP-1) in neural stem cells.

Purpose of the Study:

  • To identify the specific region on LAMP-1 responsible for FUT9-mediated Lewis X modification.
  • To determine if this region can be used to engineer Lewis X expression on other glycoproteins.

Main Methods:

  • Site-directed mutagenesis and protein sequence analysis to pinpoint the functional domain on LAMP-1.
  • In vitro and cellular assays using erythropoietin as a model glycoprotein, engineered with the identified LAMP-1 sequence.

Main Results:

  • A 29-amino acid sequence in the N-terminal domain of LAMP-1 was identified as crucial for promoting FUT9-catalyzed Lewis X modification.
  • Appending this sequence to erythropoietin successfully induced Lewis X modification both in vitro and in cultured cells.

Conclusions:

  • The identified LAMP-1 sequence functions as a specific 'Lewis X code' recognized by FUT9.
  • This code can be embedded into other proteins to direct Lewis X modification, offering novel avenues for protein and cell engineering.