Journal Article

FZJ-2020-02672

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Cold and distant: structural features of the nucleoprotein complex of a cold-adapted influenza A virus strain

Shvetsov, A. V. ; Lebedev, D. V. ; Zabrodskaya, Y. A. (Corresponding author) ; Shaldzhyan, A. A. ; Egorova, M. A. ; Vinogradova, D. S. ; Konevega, A. L. ; Gorshkov, A. N. ; Ramsay, E. S. ; Radulescu, A.FZJ* ; Sergeeva, M. V. ; Plotnikova, M. A. ; Komissarov, A. B. ; Taraskin, A. S. ; Lebedev, K. I. ; Garmay, Y. P. ; Kuznetsov, V. V. ; Isaev-Ivanov, V. V. ; Vasin, A. V. ; Tsybalova, L. M. ; Egorov, V. V.

2021
Taylor & Francis Abingdon [u.a.]

This record in other databases:    

Please use a persistent id in citations: http://hdl.handle.net/2128/28359  doi:10.1080/07391102.2020.1776636

Abstract: Two influenza A nucleoprotein variants (wild-type: G102R; and mutant: G102R and E292G) were studied with regard to macro-molecular interactions in oligomeric form (24-mers). The E292G mutation has been previously shown to provide cold adaptation. Molecular dynamics simulations of these complexes and trajectory analysis showed that the most significant difference between the obtained models was distance between nucleoprotein complex strands. The isolated complexes of two ribonucleoprotein variants were characterized by transmission electron microscopy and differential scanning fluorimetry (DSF). Presence of the E292G substitution was shown by DSF to affect nucleoprotein complex melting temperature. In the filament interface peptide model, it was shown that the peptide corresponding in primary structure to the wild-type NP (SGYDFEREGYS) is prone to temperature-dependent self-association, unlike the peptide corresponding to E292G substitution (SGYDFGREGYS). It was also shown that the SGYDFEREGYS peptide is capable of interacting with a monomeric nucleoprotein (wild type); this interaction’s equilibrium dissociation constant is five orders of magnitude lower than for the SGYDFGREGYS peptide. Using small-angle neutron scattering (SANS), the supramolecular structures of isolated complexes of these proteins were studied at temperatures of 15, 32, and 37 °C. SANS data show that the structures of the studied complexes at elevated temperature differ from the rod-like particle model and react differently to temperature changes. The data suggest that the mechanism behind cold adaptation with E292G is associated with a weakening of the interaction between strands of the ribonucleoprotein complex and, as a result, the appearance of inter-chain interface flexibility necessary for complex function at low temperature.

Keyword(s): Health and Life (1st) ; Biology (2nd) ; Soft Condensed Matter (2nd)

---

Contributing Institute(s):

1. JCNS-FRM-II (JCNS-FRM-II)
2. Heinz Maier-Leibnitz Zentrum (MLZ)
3. JCNS-4 (JCNS-4)

Research Program(s):

1. 632 - Materials – Quantum, Complex and Functional Materials (POF4-632) (POF4-632)
2. 6G4 - Jülich Centre for Neutron Research (JCNS) (FZJ) (POF4-6G4) (POF4-6G4)

Experiment(s):

1. KWS-1: Small angle scattering diffractometer (NL3b)
2. KWS-2: Small angle scattering diffractometer (NL3ao)

Appears in the scientific report 2021

---

Database coverage:
; ; ; BIOSIS Previews ; Biological Abstracts ; Clarivate Analytics Master Journal List ; Current Contents - Life Sciences ; Essential Science Indicators ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection

---