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骆驼重链抗体的出现及演化机制 被引量:1

The emergence and evolution mechanism of camel heavy chain antibody
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摘要 经典的IgG抗体由2条相同的重链(H)和2条相同的轻链(L)组成,由H链和L链共同构成抗体-抗原结合区的规则由缺失轻链和CH1区的重链抗体(heavy chain antibody,hcAb)打破。重链抗体以其分子量小,稳定性高,免疫原性弱,组织穿透力强,可以结合一些常规抗体无法接近的抗原表位等特点,显示出其与常规抗体相比在抗体-抗原结合及免疫防御中的优势。了解重链抗体是何时以及如何演化出现的对于理解这种特殊类型的抗体在机体免疫保护中的作用具有重要意义。 The classical antibodies are composed of two heavy chains (H) and two light chains (L). However, the rules which composed of the antigen-combining sites with H chain and L chain in conventional IgG antibodies were violated by the discovery of natural devoid of light chains IgG antibodies in camelids. Camel heavy chain antibodies (HCAbs) possess many interesting properties, such as potent enzyme inhibitors, the recognition of unique conformational epitopes with the dominant involvement of its long CDR3, highly soluble in aqueous environments, high stability, weak immunogenicity and smaller size, which making hcAbs promising molecules for biotechnological applications. It was worthwhile to elucidate how hcAbs response to antigen induction, and what the role of hcAbs in immune protection in camelids.
出处 《免疫学杂志》 CAS CSCD 北大核心 2013年第4期351-356,共6页 Immunological Journal
基金 新疆维吾尔自治区高技术研究发展计划项目(201110101)
关键词 骆驼 重链抗体 演化机制 免疫保护 Camel Heavy chain antibody Evolution mechanism Immune protection
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参考文献32

  • 1Hamers Casterman C, Atarhouch T, Muyldermans S, et al. Naturally occurring antibodies devoid of light chains [J]. Nature, 1993, 363(6428): 446-448.
  • 2Muyldermans S, Atarhouch T, Saldanha J, et al. Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains [J]. Protein Engng, 1994, 7(9): 1129-1135.
  • 3Yi Hui, Audrey Teh .Tony A. Kavanagh. High-level expression of Camelid nanobodies in Nicotiana benthamiana[J]. Transgenic Res, 2010, 19(4): 575-586.
  • 4Katja Conrath, Cecile Vincke, Benoit Stijlemans, et al. Antigen binding and solubility effects upon the veneering of a camel VHH in framework-2 to mimic a VH [J]. J Mol Biol, 2005, 350(1): 112-125.
  • 5Dumoulin M, Conrath K, Van Meirhaeghe A, et al. Single domain antibody fragments with high conformational stability[J]. Protein Science, 2002, 11(3): 500-515.
  • 6Harmsen MM, De Haard HJ. Properties, production, and applications of camelid single--domain antibody fragments [J]. Applied Microbiological Biotechnology, 2007, 77(1): 13-22.
  • 7Inoue H, Iihara A, Takahashi H, et al. Affinity transfer to a human protein by CDR3 grafting of camelid VHH [J]. Protein Sci, 2011, 20(12): 1971-1981.
  • 8Jahnichena S, Blanchetot S, Maussanga D, et al. CXCR4 nanobodies (VHH-based single variable domains) potently inhibit chemotaxis and HIV-1 replication and mobilize stem cells[J], Prol Natl Acad USA, 2010, 107(47): 20565- 20570.
  • 9Nguyen VK, Su C, Muyldermans S, van der Loo W. Heavy- chain antibodies in Camelidae; a case of evolutionary innovation[J]. Immunogenetics, 2003, 54(1): 39-47.
  • 10Nguyen VK, Hamers R, Wyns L, et al. Loss of splice consensus signal is responsible for the removal of the entire CH1 domain of the functional camel IgG2a heavy chain antibodies[J]. Mol Immunol, 1999, 36(8): 515-524.

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