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Shaldzhyan AA, Zabrodskaya YA, Baranovskaya IL, et al. Old dog, new tricks: Influenza A virus NS1 and in vitro fibrillogenesis. Biochimie. 2021;190:50-56doi: 10.1016/j.biochi.2021.07.005.
Shaldzhyan, A. A., Zabrodskaya, Y. A., Baranovskaya, I. L., Sergeeva, M. V., Gorshkov, A. N., Savin, I. I., Shishlyannikov, S. M., Ramsay, E. S., Protasov, A. V., Kukhareva, A. P., & Egorov, V. V. (2021). Old dog, new tricks: Influenza A virus NS1 and in vitro fibrillogenesis. Biochimie, 19050-56. https://doi.org/10.1016/j.biochi.2021.07.005
Shaldzhyan, A A, et al. "Old dog, new tricks: Influenza A virus NS1 and in vitro fibrillogenesis." Biochimie vol. 190 (2021): 50-56. doi: https://doi.org/10.1016/j.biochi.2021.07.005
Shaldzhyan AA, Zabrodskaya YA, Baranovskaya IL, Sergeeva MV, Gorshkov AN, Savin II, Shishlyannikov SM, Ramsay ES, Protasov AV, Kukhareva AP, Egorov VV. Old dog, new tricks: Influenza A virus NS1 and in vitro fibrillogenesis. Biochimie. 2021 Nov;190:50-56. doi: 10.1016/j.biochi.2021.07.005. Epub 2021 Jul 15. PMID: 34273416.
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Biochimie. 2021 Nov;190:50-56. doi: 10.1016/j.biochi.2021.07.005. Epub 2021 Jul 15.

Old dog, new tricks: Influenza A virus NS1 and in vitro fibrillogenesis.

Biochimie

A A Shaldzhyan, Y A Zabrodskaya, I L Baranovskaya, M V Sergeeva, A N Gorshkov, I I Savin, S M Shishlyannikov, E S Ramsay, A V Protasov, A P Kukhareva, V V Egorov

Affiliations

  1. Smorodintsev Research Institute of Influenza, Russian Ministry of Health, 197376, Prof. Popov 15/17, St. Petersburg, Russia; Petersburg Nuclear Physics Institute Named By B. P. Konstantinov of the National Research Center "Kurchatov Institute", 188300, mkr. Orlova Roshcha 1, Gatchina, Russia.
  2. Smorodintsev Research Institute of Influenza, Russian Ministry of Health, 197376, Prof. Popov 15/17, St. Petersburg, Russia; Petersburg Nuclear Physics Institute Named By B. P. Konstantinov of the National Research Center "Kurchatov Institute", 188300, mkr. Orlova Roshcha 1, Gatchina, Russia; National Research Centre Kurchatov Institute, 123182, Akademika Kurchatova Sq. 1, Moscow, Russia; Peter the Great St. Petersburg Polytechnic University, 194064, Polyteknicheskaya 29, St. Petersburg, Russia. Electronic address: [email protected].
  3. Smorodintsev Research Institute of Influenza, Russian Ministry of Health, 197376, Prof. Popov 15/17, St. Petersburg, Russia; Peter the Great St. Petersburg Polytechnic University, 194064, Polyteknicheskaya 29, St. Petersburg, Russia.
  4. Smorodintsev Research Institute of Influenza, Russian Ministry of Health, 197376, Prof. Popov 15/17, St. Petersburg, Russia.
  5. Smorodintsev Research Institute of Influenza, Russian Ministry of Health, 197376, Prof. Popov 15/17, St. Petersburg, Russia; All-Russia Research Institute for Food Additives - Branch of V.M. Gorbatov Federal Research Center for Food Systems of RAS, 191014, Liteyny Av. 55, St. Petersburg, Russia.
  6. Smorodintsev Research Institute of Influenza, Russian Ministry of Health, 197376, Prof. Popov 15/17, St. Petersburg, Russia; Petersburg Nuclear Physics Institute Named By B. P. Konstantinov of the National Research Center "Kurchatov Institute", 188300, mkr. Orlova Roshcha 1, Gatchina, Russia; National Research Centre Kurchatov Institute, 123182, Akademika Kurchatova Sq. 1, Moscow, Russia; Federal State Budgetary Scientific Institution "Institute of Experimental Medicine", 197376, Akademika Pavlova 12, St. Petersburg, Russia.

PMID: 34273416 DOI: 10.1016/j.biochi.2021.07.005

Abstract

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 °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.

Copyright © 2021 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved.

Keywords: Amyloid fibrils; Conformational transition; Functional amyloids; Influenza A virus; Nonstructural protein 1

Conflict of interest statement

Declaration of competing interest None.

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