期刊
BIOCHIMIE
卷 190, 期 -, 页码 50-56出版社
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.biochi.2021.07.005
关键词
Nonstructural protein 1; Influenza A virus; Amyloid fibrils; Conformational transition; Functional amyloids
资金
- NRC Kurchatov Institute [1363]
The influenza NS1 protein can form amyloid-like fibrils in vitro, with significant structural changes occurring during fibril formation. A protein fragment capable of inducing fibrillogenesis was also discovered, suggesting a potential relationship between influenza A infection and modulation of the immune response.
The influenza NS1 protein is involved in suppression of the host immune response. Recently, there is growing evidence that prion-like protein aggregation plays an important role in cellular signaling and immune responses. In this work, we obtained a recombinant, influenza A NS1 protein and showed that it is able to form amyloid-like fibrils in vitro. Using proteolysis and subsequent mass spectrometry, we showed that regions resistant to protease hydrolysis highly differ between the native NS1 form (NS1-N) and fibrillar form (NS1-F); this indicates that significant structural changes occur during fibril formation. We also found a protein fragment that is capable of inducing the process of fibrillogenesis at 37 degrees C. The discovery of the ability of NS1 to form amyloid-like fibrils may be relevant to uncovering relationships between influenza A infection and modulation of the immune response. (C) 2021 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved.
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