首页    期刊浏览 2024年07月08日 星期一
登录注册

文章基本信息

  • 标题:Biochemical and structural characterization of a recombinant fibrinogen-related lectin from Penaeus monodon
  • 本地全文:下载
  • 作者:Nongnuch Singrang ; Sirasit Laophetsakunchai ; Bich Ngoc Tran
  • 期刊名称:Scientific Reports
  • 电子版ISSN:2045-2322
  • 出版年度:2021
  • 卷号:11
  • 期号:1
  • 页码:2934
  • DOI:10.1038/s41598-021-82301-5
  • 出版社:Springer Nature
  • 摘要:Abstract Fibrinogen-related lectins are carbohydrate-binding proteins of the innate immune system that recognize glycan structures on microbial surfaces. These innate immune lectins are crucial for invertebrates as they do not rely on adaptive immunity for pathogen clearance. Here, we characterize a recombinant fibrinogen-related lectin Pm FREP from the black tiger shrimp Penaeus monodon expressed in the Trichoplusia ni insect cell. Electron microscopy and cross-linking experiments revealed that Pm FREP is a disulfide-linked dimer of pentamers distinct from other fibrinogen-related lectins. The full-length protein binds N-acetyl sugars in a Ca 2 ion-independent manner. Pm FREP recognized and agglutinated Pseudomonas aeruginosa . Weak binding was detected with other bacteria, including Vibrio parahaemolyticus , but no agglutination activity was observed. The biologically active Pm FREP will not only be a crucial tool to elucidate the innate immune signaling in P. monodon and other economically important species, but will also aid in detection and prevention of shrimp bacterial infectious diseases.
  • 其他摘要:Abstract Fibrinogen-related lectins are carbohydrate-binding proteins of the innate immune system that recognize glycan structures on microbial surfaces. These innate immune lectins are crucial for invertebrates as they do not rely on adaptive immunity for pathogen clearance. Here, we characterize a recombinant fibrinogen-related lectin Pm FREP from the black tiger shrimp Penaeus monodon expressed in the Trichoplusia ni insect cell. Electron microscopy and cross-linking experiments revealed that Pm FREP is a disulfide-linked dimer of pentamers distinct from other fibrinogen-related lectins. The full-length protein binds N-acetyl sugars in a Ca 2 ion-independent manner. Pm FREP recognized and agglutinated Pseudomonas aeruginosa . Weak binding was detected with other bacteria, including Vibrio parahaemolyticus , but no agglutination activity was observed. The biologically active Pm FREP will not only be a crucial tool to elucidate the innate immune signaling in P. monodon and other economically important species, but will also aid in detection and prevention of shrimp bacterial infectious diseases.
国家哲学社会科学文献中心版权所有