Functional expression of the Fc-fused extracellular domains of group II membrane proteins

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• 作者：Weicheng Wu (1)
  Jing Jin (3)
  Xiaojuan Liu (1) (6)
  Yufei Zhang (4)
  Meng Li (5)
  Miaomiao Shao (1)
  Yifan Qian (1)
  Dongmei Zhang (1)
  Haiyan Zhu (1)
  Yuanyuan Ruan (1)
  Jianhui Xie (1) (2)
  Jianxin Gu (1)
  
  1. Key Laboratory of Glycoconjugate Research ; Ministry of Health ; Department of Biochemistry and Molecular Biology ; Shanghai Medical College ; Fudan University ; Shanghai ; 200032 ; China
  3. Institute of Glycobiological Engineering ; Zhejiang Provincial Key Laboratory of Medical Genetics ; Wenzhou Medical College ; Wenzhou ; 325035 ; China
  6. Department of Pathogen Biology ; Medical College ; Nantong University ; Nantong ; Jiangsu ; 226001 ; China
  4. Department of Immunology ; Shanghai Medical College ; Fudan University ; Shanghai ; 200032 ; China
  5. Department of Dermatology ; Shanghai Key Laboratory of Molecular ; Mycology & PLA Key Laboratory of Fungal Diseases ; Changzheng Hospital ; Second Military Medical University ; Shanghai ; 200032 ; China
  2. Department of Forensic Medicine ; Shanghai Medical College ; Fudan University ; Shanghai ; 200032 ; China
  
• 关键词：Fc moiety ; Extracellular domain ; Group II membrane proteins ; CLEC ; 2
• 刊名：Glycoconjugate Journal
• 出版年：2015
• 出版时间：February 2015
• 年：2015
• 卷：32
• 期：1-2
• 页码：69-76
• 全文大小：2,132 KB
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• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Biochemistry
  Pathology
  
• 出版者：Springer Netherlands
• ISSN：1573-4986

文摘

The complicated delivery mechanism of group II membrane proteins makes it difficult to decide the fusion pattern of their extracellular domains (ECDs) with Fc moiety. In this study, we compared the expression of ECDs of three group II membrane proteins including CLEC-2, Dectin-1, and LOX-1 by fusion of Fc moiety. We found that the pattern of ECD-Fc fusion order produced the functionally active recombinant proteins while the pattern of Fc-ECD fusion order led to the altered glycosylation which abolished the binding of these proteins with their ligands. Meanwhile, our results indicated that the secretion of mouse Fc (mFc)-fused ECD of CLEC-2 was more efficient than that of rabbit Fc (rFc)-fused protein, while rFc moiety was more sensitive for detection compared with mFc moiety. Altogether, we provide a favorable fusion pattern of Fc moiety with the ECDs of group II transmembrane proteins.