Gonzalez-Sapienza Gualberto, Rossotti Martín A, Tabares-da Rosa Sofía
Cátedra de Inmunología, Facultad de Química, Instituto de Higiene, UDELAR, Montevideo, Uruguay.
Front Immunol. 2017 Aug 21;8:977. doi: 10.3389/fimmu.2017.00977. eCollection 2017.
With just three CDRs in their variable domains, the antigen-binding site of camelid heavy-chain-only antibodies (HcAbs) has a more limited structural diversity than that of conventional antibodies. Even so, this does not seem to limit their specificity and high affinity as HcAbs against a broad range of structurally diverse antigens have been reported. The recombinant form of their variable domain [nanobody (Nb)] has outstanding properties that make Nbs, not just an alternative option to conventional antibodies, but in many cases, these properties allow them to reach analytical or diagnostic performances that cannot be accomplished with conventional antibodies. These attributes include comprehensive representation of the immune specificity in display libraries, easy adaptation to high-throughput screening, exceptional stability, minimal size, and versatility as affinity building block. Here, we critically reviewed each of these properties and highlight their relevance with regard to recent developments in different fields of immunosensing applications.
骆驼科仅重链抗体(HcAbs)的可变结构域中只有三个互补决定区(CDRs),其抗原结合位点的结构多样性比传统抗体更有限。即便如此,这似乎并未限制它们的特异性和高亲和力,因为已有报道称HcAbs可针对多种结构多样的抗原。其可变结构域的重组形式[纳米抗体(Nb)]具有出色的特性,这使得纳米抗体不仅是传统抗体的替代选择,而且在许多情况下,这些特性使它们能够达到传统抗体无法实现的分析或诊断性能。这些特性包括在展示文库中全面呈现免疫特异性、易于适应高通量筛选、卓越的稳定性、极小的尺寸以及作为亲和力构建模块的多功能性。在此,我们对这些特性逐一进行了批判性综述,并强调了它们与免疫传感应用不同领域近期发展的相关性。