固态核磁共振光谱显示，HET-s(218 - 289)的大肠杆菌包涵体是淀粉样蛋白。
Solid-state NMR spectroscopy reveals that E. coli inclusion bodies of HET-s(218-289) are amyloids.
作者信息
Wasmer Christian, Benkemoun Laura, Sabaté Raimon, Steinmetz Michel O, Coulary-Salin Bénédicte, Wang Lei, Riek Roland, Saupe Sven J, Meier Beat H
机构信息
Laboratorium für Physikalische Chemie, ETH Zurich, 8093 Zurich, Switzerland.
出版信息
Angew Chem Int Ed Engl. 2009;48(26):4858-60. doi: 10.1002/anie.200806100.
Protein deposition frequently occurs as inclusion bodies (IBs) during heterologous protein expression in E. coli. The structure of these E. coli IBs of the prion-forming domain from the fungal prion HET-s is the same as that previously determined for fibrils assembled in vitro, and show prion infectivity. These results demonstrate that the IBs of HET-s(218-289) are amyloids.
在大肠杆菌中进行异源蛋白表达时，蛋白质沉积经常以包涵体（IBs）的形式出现。来自真菌朊病毒HET-s的朊病毒形成结构域的这些大肠杆菌包涵体的结构与先前在体外组装的纤维所确定的结构相同，并显示出朊病毒感染性。这些结果表明，HET-s(218-289)的包涵体是淀粉样蛋白。
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