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本文引用的文献

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The multicompartmental p32/gClqR as a new target for antibody-based tumor targeting strategies.多腔 p32/gClqR 作为一种新的基于抗体的肿瘤靶向策略的靶标。
J Biol Chem. 2011 Feb 18;286(7):5197-203. doi: 10.1074/jbc.M110.161927. Epub 2010 Dec 14.
2
Crystal structure of the human collagen XV trimerization domain: a potent trimerizing unit common to multiplexin collagens.人胶原蛋白 XV 三聚化结构域的晶体结构：多联素胶原蛋白的一个有效三聚化单位。
Matrix Biol. 2011 Jan;30(1):9-15. doi: 10.1016/j.matbio.2010.09.005. Epub 2010 Oct 13.
3
Multivalent antibodies: when design surpasses evolution.多价抗体：设计超越进化。
Trends Biotechnol. 2010 Jul;28(7):355-62. doi: 10.1016/j.tibtech.2010.03.007. Epub 2010 May 4.
4
Tumor-associated and microbial proteases compromise host IgG effector functions by a single cleavage proximal to the hinge.肿瘤相关蛋白酶和微生物蛋白酶通过在铰链区附近的单次切割损害宿主IgG效应功能。
Proc Natl Acad Sci U S A. 2009 Oct 20;106(42):17864-9. doi: 10.1073/pnas.0904174106. Epub 2009 Oct 7.
5
Crystal structure of human collagen XVIII trimerization domain: A novel collagen trimerization Fold.人胶原蛋白 XVIII 三聚化结构域的晶体结构：一种新型的胶原蛋白三聚化折叠。
J Mol Biol. 2009 Sep 25;392(3):787-802. doi: 10.1016/j.jmb.2009.07.057. Epub 2009 Jul 23.
6
In vivo tumor targeting and imaging with engineered trivalent antibody fragments containing collagen-derived sequences.利用含有胶原蛋白衍生序列的工程化三价抗体片段进行体内肿瘤靶向与成像。
PLoS One. 2009;4(4):e5381. doi: 10.1371/journal.pone.0005381. Epub 2009 Apr 29.
7
Enhanced antiangiogenic therapy with antibody-collagen XVIII NC1 domain fusion proteins engineered to exploit matrix remodeling events.通过设计利用基质重塑事件的抗体-胶原蛋白XVIII NC1结构域融合蛋白增强抗血管生成疗法。
Int J Cancer. 2006 Jul 15;119(2):455-62. doi: 10.1002/ijc.21851.
8
Engineered antibody fragments and the rise of single domains.工程化抗体片段与单域抗体的兴起。
Nat Biotechnol. 2005 Sep;23(9):1126-36. doi: 10.1038/nbt1142.
9
Antibody engineering: facing new challenges in cancer therapy.抗体工程：癌症治疗面临的新挑战
Acta Pharmacol Sin. 2005 Jun;26(6):641-8. doi: 10.1111/j.1745-7254.2005.00135.x.
10
Proteoglycan-collagen XV in human tissues is seen linking banded collagen fibers subjacent to the basement membrane.在人体组织中，蛋白聚糖 - 胶原蛋白XV可见于连接基底膜下方的带状胶原纤维。
J Histochem Cytochem. 2005 Feb;53(2):165-76. doi: 10.1369/jhc.4A6376.2005.

包含人胶原蛋白XV三聚化结构域的多价抗体的稳定性提高。

Improved stability of multivalent antibodies containing the human collagen XV trimerization domain.

作者信息

Cuesta Angel M, Sánchez-Martín David, Blanco-Toribio Ana, Villate Maider, Enciso-Álvarez Kelly, Alvarez-Cienfuegos Ana, Sainz-Pastor Noelia, Sanz Laura, Blanco Francisco J, Alvarez-Vallina Luis

机构信息

Madrid, Spain; Molecular Immunology Unit; Hospital Universitario Puerta de Hierro.

Madrid, Spain; Leadartis S.L., Ferraz 3.

出版信息

MAbs. 2012 Mar-Apr;4(2):226-32. doi: 10.4161/mabs.4.2.19140. Epub 2012 Mar 1.

DOI:10.4161/mabs.4.2.19140
PMID:22453098
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3361658/
Abstract

We recently described the in vitro and in vivo properties of an engineered homotrimeric antibody made by fusing the N-terminal trimerization region of collagen XVIII NC1 domain to the C-terminus of a scFv fragment [trimerbody (scFv-NC1) 3; 110 kDa]. Here, we demonstrated the utility of the N-terminal trimerization region of collagen XV NC1 domain in the engineering of trivalent antibodies. We constructed several scFv-based trimerbodies containing the human type XV trimerization domain and demonstrated that all the purified trimerbodies were trimeric in solution and exhibited excellent antigen binding capacity. Importantly, type XV trimerbodies demonstrated substantially greater thermal and serum stability and resistance to protease digestion than type XVIII trimerbodies. In summary, the small size, high expression level, solubility and stability of the trimerization domain of type XV collagen make it the ideal choice for engineering homotrimeric antibodies for cancer detection and therapy.

摘要

我们最近描述了一种工程化同源三聚体抗体的体外和体内特性，该抗体是通过将胶原蛋白 XVIII NC1 结构域的 N 端三聚化区域融合到单链抗体片段（scFv）的 C 端而制成的[三聚体抗体（scFv-NC1）3；110 kDa]。在此，我们展示了胶原蛋白 XV NC1 结构域的 N 端三聚化区域在三价抗体工程中的效用。我们构建了几种包含人 XV 型三聚化结构域的基于 scFv 的三聚体抗体，并证明所有纯化的三聚体抗体在溶液中均为三聚体，且表现出优异的抗原结合能力。重要的是，XV 型三聚体抗体在热稳定性和血清稳定性以及对蛋白酶消化的抗性方面比 XVIII 型三聚体抗体有显著提高。总之，XV 型胶原蛋白三聚化结构域的小尺寸、高表达水平、溶解性和稳定性使其成为用于癌症检测和治疗的同源三聚体抗体工程的理想选择。