Laboratory for Environmental and Life Sciences, University of Nova Gorica, Vipavska Cesta 13, 5000 Nova Gorica, Slovenia.
Institut de Biotecnologia i de Biomedicina (IBB), Carrer de la Vall Moronta s/n, Universitat Autònoma de Barcelona, 08193 Cerdanyola del Vallès, Spain.
FEMS Microbiol Rev. 2019 Jan 1;43(1):53-72. doi: 10.1093/femsre/fuy038.
Understanding the structure, functionalities and biology of functional amyloids is an issue of emerging interest. Inclusion bodies, namely protein clusters formed in recombinant bacteria during protein production processes, have emerged as unanticipated, highly tunable models for the scrutiny of the physiology and architecture of functional amyloids. Based on an amyloidal skeleton combined with varying amounts of native or native-like protein forms, bacterial inclusion bodies exhibit an unusual arrangement that confers mechanical stability, biological activity and conditional protein release, being thus exploitable as versatile biomaterials. The applicability of inclusion bodies in biotechnology as enriched sources of protein and reusable catalysts, and in biomedicine as biocompatible topographies, nanopills or mimetics of endocrine secretory granules has been largely validated. Beyond these uses, the dissection of how recombinant bacteria manage the aggregation of functional protein species into structures of highly variable complexity offers insights about unsuspected connections between protein quality (conformational status compatible with functionality) and cell physiology.
理解功能型淀粉样蛋白的结构、功能和生物学特性是一个新兴的研究课题。包涵体，即在重组细菌中蛋白质生产过程中形成的蛋白质聚集体，已成为研究功能型淀粉样蛋白的生理学和结构的一种出人意料的、高度可调的模型。基于淀粉样的骨架和不同数量的天然或类似天然的蛋白质形式，细菌包涵体表现出一种不寻常的排列方式，赋予了它们机械稳定性、生物活性和条件性蛋白质释放能力，因此可以作为多功能生物材料进行开发。包涵体在生物技术中的应用，如作为富含蛋白质的来源和可重复使用的催化剂，以及在生物医学中的应用，如作为生物相容性的拓扑结构、纳米颗粒或内分泌分泌颗粒的模拟物，已经得到了广泛的验证。除此之外，研究重组细菌如何将功能性蛋白质聚集成高度可变复杂结构的过程，揭示了蛋白质质量（与功能兼容的构象状态）和细胞生理学之间意想不到的联系。
