On the structural features of influenza A nucleoprotein particles from small-angle X-ray scattering data

Егоров, Владимир В.; Shaldzhyan, Aram A.; Горшков, А. Н.; Zabrodskaya, Yana A.; Лебедев, Д. В.; Куклин, А. И.; Ksenofontova, O. I.; Швецов, А. В.; Васин, А. В.; Цыбалова, Л. М.; Isaev-Ivanov, V. V.

doi:10.1134/s1027451016020063

Cited by 6 publications

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“…In addition, the ability of the double protein helix to unwind and other significant changes in RNP helical structure have been shown [18]. We have previously published differences in RNP structure in solution at room temperature (22°C) and operating temperature (37°C), according to small-angle X-ray scattering data [15]. It is important to note that in different strains featuring different reproduction temperature characteristics, various molecular mechanisms may be behind the coldadapted phenotype.…”

Section: Resultsmentioning

confidence: 99%

“…RNPs Isolation of influenza A H3N2 virus (A/Hong Kong/68) ribonucleoprotein complexes was carried out using a viral suspension kindly provided by the Smorodintsev Research Institute of Influenza's Influenza Vaccine Laboratory, following published methods [14]. Identification of the NP-containing fractions was carried out using described Western blotting methods [15]. For SANS, the protein was transferred to a heavy water buffer.…”

Section: Methodsmentioning

confidence: 99%

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Cold and distant: structural features of the nucleoprotein complex of a cold-adapted influenza A virus strain

Швецов

Лебедев

Zabrodskaya

et al. 2020

Journal of Biomolecular Structure and Dynamics

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Two influenza A nucleoprotein variants (wt: 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 differences between nucleoprotein complex strands. Influenza virus nucleoprotein complexes were isolated from strains bearing the corresponding NP amino acid substitutions. The isolated complexes 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, wild type peptide) is prone to temperature-dependent selfassociation, unlike the peptide carrying the substitution corresponding to E292G (SGYDFGREGYS, mutant peptide). It was also shown that the SGYDFEREGYS peptide (wt) is capable of interacting with a recombinant full-size monomeric nucleoprotein (with primary structure corresponding to 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 was studied at temperatures of 15, 32, and 37°C. SANS data show that the structures of the studied complexes (mutant or normal proteins with RNA) 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 interchain interface flexibility necessary for complex function at low temperature..

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%