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首页> 外文期刊>Journal of Molecular Biology >Structural Basis of Epitope Recognition by Heavy-Chain Camelid Antibodies
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Structural Basis of Epitope Recognition by Heavy-Chain Camelid Antibodies

机译：重链骆驼抗体表位识别的结构基础

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摘要

Truncated versions of heavy-chain antibodies (HCAbs) from camelids, also termed nanobodies, comprise only one-tenth the mass of conventional antibodies, yet retain similar, high binding affinities for the antigens. Here we analyze a large data set of nanobody–antigen crystal structures and investigate how nanobody–antigen recognition compares to the one by conventional antibodies. We find that nanobody paratopes are enriched in aromatic residues just like conventional antibodies, but additionally, they also bear a more hydrophobic character. Most striking differences were observed in the characteristics of the antigen's epitope. Unlike conventional antibodies, nanobodies bind to more rigid, concave, conserved and structured epitopes enriched with aromatic residues. Nanobodies establish fewer interactions with the antigens compared to conventional antibodies, and we speculate that high binding affinities are achieved due to less unfavorable conformational and more favorable solvation entropy contributions. We observed that interactions with antigen are mediated not only by three CDR loops but also by numerous residues from the nanobody framework. These residues are not distributed uniformly; rather, they are concentrated into four structurally distinct regions and mediate mostly charged interactions. Our findings suggest that in some respects nanobody–antigen interactions are more similar to the general protein–protein interactions rather than antibody–antigen interactions.
机译：来自骆驼的重链抗体（HCABs）的截短的版本，也称为纳米甲基，仅包含常规抗体的质量，但保持相似的抗原的高结合亲和力。在这里，我们分析了一种大数据集的纳米抗体 - 抗原晶体结构，并研究纳米体 - 抗原识别如何通过常规抗体对其进行比较。我们发现纳米体估伏在芳族残留物中，就像常规抗体一样，但另外，它们也承受更疏水的特征。在抗原表位的特征中观察到最引人注目的差异。与常规抗体不同，纳米甲基odies结合富含芳族残基的更加刚性，凹，保守的和结构化表位。与常规抗体相比，纳米级与抗原建立较少的相互作用，并且我们推测由于不利的构象和更有利的溶剂化熵贡献，因此实现了高结合亲和力。我们观察到与抗原的相互作用不仅介导三个CDR环，而且由来自纳米级框架的许多残基进行介导。这些残留物不均匀分布;相反，它们集中成四个结构上不同的区域，并介导大多数充电的相互作用。我们的研究结果表明，在一些方面，纳米抗体 - 抗原相互作用与普通蛋白质 - 蛋白质相互作用更类似于抗体 - 抗原相互作用。

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