RT Journal Article
SR Electronic
T1 Old Dog, New Tricks: Influenza A Virus NS1 and <em>In Vitro</em> Fibrillogenesis
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2020.08.17.254060
DO 10.1101/2020.08.17.254060
A1 A.A. Shaldzhyan
A1 Y.A. Zabrodskaya
A1 I.L. Baranovskaya
A1 M.V. Sergeeva
A1 A.N. Gorshkov
A1 I.I. Savin
A1 S.M. Shishlyannikov
A1 E.S. Ramsay
A1 A.V. Protasov
A1 A.P. Kukhareva
A1 V.V. Egorov
YR 2020
UL http://biorxiv.org/content/early/2020/08/17/2020.08.17.254060.abstract
AB 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. 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.Competing Interest StatementThe authors have declared no competing interest.