FOOD SCIENCE ›› 2013, Vol. 34 ›› Issue (3): 294-297.
Previous Articles Next Articles
Received:
2011-12-29
Revised:
2013-01-10
Online:
2013-02-15
Published:
2017-12-29
Contact:
Liang Ma
E-mail:zhyhml@163.com
CLC Number:
[1] 吴石金, 孙培龙. 简明免疫学原理[M]. 北京: 化学工业出版社, 2008: 173.[2] 冯仁青, 郭振泉. 现代抗体技术及其应用[M]. 北京: 北京大学出版社, 2006: 55,76.[3] 胡圣尧. 免疫学与生物技术[M]. 北京: 人民卫生出版社, 2003: 61.[4] Gibbs WW. Nanobodies [J]. Sci Am, 2005, 293: 78-83.[5] Hamers-Casteman C, Atarhouch T, Muyldemans S, et al. Naturally occurring antibodies devoid of light chains [J]. Nature, 1993, 363(6428): 446-448.[6] Nguyen 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.[7] 李国秀, 李建科. 纳米技术在食品领域中的应用[J]. 粮食与油脂, 2007, 8: 13.[8] Muyldermans S, Lauwereys M. Unique single-domain antigen binding fragments derived from naturally occurring camel heavy-chain antibodies [J]. Mol Recognit, 1999, 12: 1-10.[9] De Genst E, Silence K, Decanniere K,et al. Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies[J]. PNAS, 2006, 103: 4586–4591.[10] Vincke C, Loris R, Saerens D, Martinez-Rodriguez S, et al. General strategy to humanize a camelid single-domain antibody and identification of a universal humanized nanobody scaffold[J]. J Bio Chem, 2009, 284:3273-3284.[11] Muyldermans 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 Eng, 1994, 7(9): 1129-1135.[12] Vu, K.B, Ghahroudi, M A., Wyns, L, Muyldermans, S. Comparison of llama VH sequences from conventional and heavy chain antibodies[J]. Mol. Immunol, 1997, 34: 1121–1131.[13] Wu, T T , Johnson, G, Kabat, E A. Length distribution of CDR H3 in antibodies[J]. Proteins: Struct. Funct. Genetics ,1993,16: 1-7.[14] Nguyen V K, Desmyter A , Muyldermans S, et al. Functional heavy-chain antibodies in Camelidae [J]. Adv. Immunol, 2001,79: 261-296.[15] Davies J, Riechmann L. Camelising human antibody fragments: NMR studies on VH domains [J]. FEBS Letters, 1994, 339(3): 285-290.[16] Ghahroudi M A, Desmyter A, Wyns L, et a1.Selection and identification of single domain antibody fragments from camel heavy-chain antibodies[J]. FEBS Lett, 1997, 414: 521-526.[17] Vander Linden RH, Frenken LG, de Geus B, et al. Comparison of physical chemical properties of llama VHH antibody fragments and mouse monoclonaI antibodies[J]. Biochim Biophys Acta, 1999, 1431: 37-46.[18] 秦海燕, 毛晓燕, 乔玉玲, 等. 单链抗体的研究进展[J]. 现代生物医学进展, 2011, 11(4): 795-797.[19] Pe′rez J M J, Renisio J G, Prompers JJ, van Platernik C J, et al. Thermal unfolding of a llama antibody fragment: a two-state reversible process[J]. Biochemistry, 2001, 40: 74–83.[20] Ewert S, Cambillau C, Conrath K, Plu¨ckthun A. Biophysical properties of camelid VHH domains compared to those of human VH3 domains[J]. Biochemistry, 2002, 41: 3628–3636.[21] Dumoulin M, Courath K, Van Meirhaeqhe A, et al. Single domain antibody fragments with high conformational stability [J]. Protein Sci, 2002, 11(3): 500-515.[22] Stijlemans B, Conrath K, Cortez-Retamozo V, et al. Efficient targeting of conserved cryptic epitopes of infectious agents by single-domain antibodies. African trypanosomes as a paradigm [J]. J Biol Chem, 2004, 279(2): 1256-1261.[23] Cortez-Retamozo V, Backmann N, Senter PD, et al. Efficient cancer therapy with a nanobody-based conjugate[J]. Cancer Res, 2004, 64(8) :2853- 2857. [24] 苏幼红, 李江伟. 骆驼来源单域抗体在免疫治疗中的研究进展[J]. 生物技术通报, 2010, 6: 27-32. [25] Cortez-Retamozo V, Lauwereys M, Hassanzadeh Gh G, et a1. Efficient tumor targeting by single-domain antibody fragments of Camels[J]. Int J Cancer, 2002, 98: 456-462.[26] aneycken I, D’huyvetter M, Hernot S, et al. Immuno-imaging using nanobodies[J]. Current Opinion in Biotechnology, 2011, 22: 877-881.[27] Vaneycken I, Xavier C, Blykers A, et al. Synthesis and first in vivo evaluation of 18F-anti-HER2-nanobodies: a new probe for PET imaging of HER2 expression in breast cancer[J]. J Nucl Med, 2011, 52: 664-1664.[28] Harmsen M M, de Haard H J. Properties, production, and applications of camelid single-domain antibody fragments[J]. Appl Microbiol Biotechnol, 2007, 77: 13-22.[29] 涂追, 许杨, 何庆华, 等. 半巢式PCR法构建天然噬菌体单域重链抗体文库[J]. 食品科学, 2010, 31(19): 299-303.[30] Cortez-Retamozo V, Backmann N, Senter P D, et al. Efficient cancer therapy with a nanobody-based conjugate[J]. Cancer Ras, 2004, 64: 2853-2857.[31] Oliveira S, Raymond M. Schiffelers, Joris van der Veeken, et al. Downregulation of EGFR by a novel multivalent nanobody-liposome platform[J]. Journal of Controlled Release, 2010, 145: 165-175.[32] Muyldermans S, Baral T N, Cortez Retamozzo V, et al. Camelid immunoglobulins and nanobody technology[J]. Veterinary Immunology and Immunopathology, 2009, 128: 178-183.[33] Behar G, Sibéril S, Groulet A, et al. Isolation and characterization of anti-FcgammaRIII (CD16) llama singledomain antibodies that activate natural killer cells [J]. Protein Eng DesSel, 2008, 21: 1210.[34] Abbady A Q, Al-Mariri A, Zarkawi M, et al. Evaluation of a nanobody phage display library constructed from a Brucella-immunised camel[J]. Veterinary Immunology and Immunopathology, 2011, 142: 49-56.[35] Steyaert J, Kobila K. Nanobody stabilization of G protein-coupled receptor conformational states[J]. Current Opinion in Structural Biology, 2011, 21: 567-572.[36] Skottrup P D, Leonard P, Kaczmarek J Z, et al. Diagnostic evaluation of a nanobody with picomolar affinity toward the protease RgpB from Porphyromonas gingivalis[J]. Analytical Biochemistry, 2011, 415: 158-167.[37] Pleschberger M, Saerens D, Weigert S, et al. An S-layer heavychain camel antibody fusion protein for generating of a nanopatterned sensing layer to detect the prostate specific antigen by surface plasmon resonance technique [J]. Bioconjug Chem, 2004, 15(3): 664-671.[38] Hmila I, Abdallah RBA, Saerens D, et al. VHH, bivalent domains and chimeric heavy chain-only antibodies with high neutralizing efficacy for scorpion toxin AahI,[J]. Mol. Immunol, 2008, 45: 3847-3856.[39] 汤俊琪, 庞广昌. 免疫传感器测定食品中的黄曲霉毒素的研究进展[J]. 食品科学, 2009, 30(17): 318-329.[40] 王铁斌, 丁虎生, 杨炼, 等. 抗黄曲霉毒素B1单链抗体的筛选和鉴定[J]. 微生物学报, 2009, 49(1): 135-140.[41] 杨炼, 刘自琴, 刘蓉, 等. 抗黄曲霉毒素B1单链抗体的表达载体的比较[J]. 食品科学, 2010, 31(09): 171-176.[42] 刘蓉, 杨炼, 孙秀兰, 等. 应用抗黄曲霉毒素单链抗体检测酱油中黄曲霉毒素B1[J]. 食品工业科技, 2011, 32(1): 281-283.[43] 管笛, 李培武, 张奇, 等. 黄曲霉毒素B1标准替代物的制备及其在花生样品检测中的应用[J]. 中国油料作物学报, 2011, 33(5): 503-506.[44] 王弘, 刘细霞, 潘科, 等. 抗克伦特罗单链抗体基因构建及蛋白结构模拟[J]. 食品科学, 2009, 30(13): 227-231.[45] 刘细霞, 孙远明, 董洁娴, 等. 抗克伦特罗核糖体展示单链抗体文库的构建及鉴定[J]. 食品科学, 2011, 32(15): 200-204.[46] 贺江, 梁颖, 樊明涛, 等. 噬菌体展示技术制备甲氧基有机磷农药抗独特型抗体[J]. 分析化学研究报告, 2011, 39(2): 178-182.[47] 王俊平, 张伟伟, 杜欣军, 等. 西维因单链抗体基因克隆、表达及活性分析[J]. 食品工业科技, 2010, 31(11): 161-164.[48] 齐永华, 董永军, 宁红梅, 等. 单链抗体技术在农兽药残留检测方面的研究进展[J]. 东北农业大学学报, 2011, 49(9): 7-11.[49] Kirchhofer A, Helma J, Schmidthals K, et al. Modulation of protein properties in living cells using nanobodies[J]. Nat. Struct. Mol. Biol, 2009, 17: 133–138. |
Viewed | ||||||
Full text |
|
|||||
Abstract |
|
|||||