+検索条件
-Structure paper
タイトル | Cryo-EM structure and polymorphic maturation of a viral transduction enhancing amyloid fibril. |
---|---|
ジャーナル・号・ページ | Nat Commun, Vol. 14, Issue 1, Page 4293, Year 2023 |
掲載日 | 2023年7月18日 |
![]() | Thomas Heerde / Desiree Schütz / Yu-Jie Lin / Jan Münch / Matthias Schmidt / Marcus Fändrich / ![]() |
PubMed 要旨 | Amyloid fibrils have emerged as innovative tools to enhance the transduction efficiency of retroviral vectors in gene therapy strategies. In this study, we used cryo-electron microscopy to analyze ...Amyloid fibrils have emerged as innovative tools to enhance the transduction efficiency of retroviral vectors in gene therapy strategies. In this study, we used cryo-electron microscopy to analyze the structure of a biotechnologically engineered peptide fibril that enhances retroviral infectivity. Our findings show that the peptide undergoes a time-dependent morphological maturation into polymorphic amyloid fibril structures. The fibrils consist of mated cross-β sheets that interact by the hydrophobic residues of the amphipathic fibril-forming peptide. The now available structural data help to explain the mechanism of retroviral infectivity enhancement, provide insights into the molecular plasticity of amyloid structures and illuminate the thermodynamic basis of their morphological maturation. |
![]() | ![]() ![]() ![]() |
手法 | EM (らせん対称) |
解像度 | 2.86 Å |
構造データ | EMDB-16930, PDB-8okr: |
由来 |
|
![]() | PROTEIN FIBRIL / virus enhancing amyloid fibril / prion |