Golovko AO, et al. Aggregation of Influenza A Virus Nuclear Export Protein. Biochemistry (Mosc). 2018 Nov;83
Influenza A virus nuclear export protein (NEP) plays an important role in the viral life cycle. Recombinant NEP proteins containing (His)6-tag at either N- or C-terminus were obtained by heterologous expression in Escherichia coli cells and their high propensity for aggregation was demonstrated. Dynamic light scattering technique was used to study the kinetics and properties of NEP aggregation in solutions under different conditions (pH, ionic strength, presence of low-molecular-weight additives and organic solvents). Using atomic force microscopy, the predominance of spherical aggregates in all examined NEP preparations was shown, with some amyloid-like structures being observed in the case of NEP-C protein. A number of structure prediction programs were used to identify aggregation-prone regions in the NEP structure. All-atom molecular dynamics simulations indicate a high rate of NEP molecule aggregation and reveal the regions preferentially involved in the intermolecular contacts that are located at the edges of the rod-like protein molecule. Our results suggest that NEP aggregation is determined by different types of interactions and represents an intrinsic property of the protein that appears to be necessary for its functioning in vivo.
See Also:
Latest articles in those days:
- Phylogeography and gene pool analysis of highly pathogenic avian influenza H5N1 viruses reported in India from 2006 to 2021 44 minute(s) ago
- Analysis of a diffusive epidemic model with a zero-infection zone 2 hours ago
- Quick detection of H5N1 avian influenza virus by surface enhanced Raman scattering(SERS) using aptamer capture 2 hours ago
- The critical role of RAGE in severe influenza infection: A target for control of inflammatory response in the disease 2 hours ago
- Human infection caused by avian influenza A (H10N5) virus 2 hours ago
[Go Top] [Close Window]