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Abstract <p>Lectins of the Legume family have been identified as carbohydrate-binding proteins for a long time. However, despite long-standing and intensive research, there is insufficient information on the role of lectins of this family in the processes of normal plant cell physiology. Analysis of transcriptomic data of flax stem tissues [1] previously revealed the differential expression pattern of lectin genes of different families. Among lectins with increased gene expression levels in tissues with a primary cell wall, three representatives of the Legume family were identified. For one of them, Lus10021117, was optimized a method for producing the recombinant protein in plant expression system <i>Nicotiana benthamiana</i>. We report the identification of several glycoforms of the recombinant protein. One of this glycoform was found to form dimers stabilized by weak, non-covalent interactions. Furthermore, phosphorylation was first experimentally demonstrated for this protein.</p>

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Recombinant Flax Lectin from Legume Family: Structure Modeling and Analysis of Posttranslational Modifications

  • 期刊论文

  • 发表日期：

    2025年12月1日

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  • N. Petrova,
  • N. Syrchina,
  • N. Mokshina

摘要

Abstract

Lectins of the Legume family have been identified as carbohydrate-binding proteins for a long time. However, despite long-standing and intensive research, there is insufficient information on the role of lectins of this family in the processes of normal plant cell physiology. Analysis of transcriptomic data of flax stem tissues [1] previously revealed the differential expression pattern of lectin genes of different families. Among lectins with increased gene expression levels in tissues with a primary cell wall, three representatives of the Legume family were identified. For one of them, Lus10021117, was optimized a method for producing the recombinant protein in plant expression system Nicotiana benthamiana. We report the identification of several glycoforms of the recombinant protein. One of this glycoform was found to form dimers stabilized by weak, non-covalent interactions. Furthermore, phosphorylation was first experimentally demonstrated for this protein.