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000878184 1001_ $$00000-0003-1140-5751$$aShvetsov, A. V.$$b0
000878184 245__ $$aCold and distant: structural features of the nucleoprotein complex of a cold-adapted influenza A virus strain
000878184 260__ $$aAbingdon [u.a.]$$bTaylor & Francis$$c2021
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000878184 520__ $$aTwo 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.
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000878184 7001_ $$00000-0003-4313-9953$$aLebedev, D. V.$$b1
000878184 7001_ $$00000-0003-2012-9461$$aZabrodskaya, Y. A.$$b2$$eCorresponding author
000878184 7001_ $$00000-0002-8646-6252$$aShaldzhyan, A. A.$$b3
000878184 7001_ $$00000-0003-1408-8413$$aEgorova, M. A.$$b4
000878184 7001_ $$0P:(DE-HGF)0$$aVinogradova, D. S.$$b5
000878184 7001_ $$00000-0003-0125-7150$$aKonevega, A. L.$$b6
000878184 7001_ $$00000-0003-2303-1144$$aGorshkov, A. N.$$b7
000878184 7001_ $$0P:(DE-HGF)0$$aRamsay, E. S.$$b8
000878184 7001_ $$0P:(DE-Juel1)130905$$aRadulescu, Aurel$$b9
000878184 7001_ $$00000-0003-0411-9896$$aSergeeva, M. V.$$b10
000878184 7001_ $$00000-0001-8196-3156$$aPlotnikova, M. A.$$b11
000878184 7001_ $$00000-0003-1733-1255$$aKomissarov, A. B.$$b12
000878184 7001_ $$00000-0003-2235-9658$$aTaraskin, A. S.$$b13
000878184 7001_ $$00000-0002-8710-6136$$aLebedev, K. I.$$b14
000878184 7001_ $$0P:(DE-HGF)0$$aGarmay, Yu. P.$$b15
000878184 7001_ $$0P:(DE-HGF)0$$aKuznetsov, V. V.$$b16
000878184 7001_ $$00000-0002-4593-1971$$aIsaev-Ivanov, V. V.$$b17
000878184 7001_ $$00000-0002-1391-7139$$aVasin, A. V.$$b18
000878184 7001_ $$00000-0002-1193-5907$$aTsybalova, L. M.$$b19
000878184 7001_ $$00000-0002-3670-8962$$aEgorov, V. V.$$b20
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