Share This Author
Localization of the influenza virus nucleoprotein: cell-associated and extracellular non-virion forms.
Comparative analysis of the kinetics of the accumulation of NP in the supernatant of infected cells, on the cell surface and inside the cells in relation to virus production, showed that there is a significant correlation between them.
Intracellular oligomerization of influenza virus nucleoprotein.
It is shown that boiling-sensitive NP oligomers (di- and trimers) are formed in vivo in the course of intracellular influenza virus replication and the possibility is discussed that oligomeric NP is a native and functionally significant form of influenza virus NP.
Stability of intracellular influenza virus nucleocapsid protein oligomers
It was shown that intrachain disulfides revealed in nascent NPs are reduced in NP subunits of NP oligomers, and this probably contributes to the stability and compactness of the oligomers.
An antigenic epitope of influenza virus nucleoprotein (NP) associated with polymeric forms of NP
The results obtained suggest that in vivo formation and in vitro renaturation of the N5D3 epitope depend on inter-subunit interactions of monomeric NPs and NP-NP interactions influence the antigenic structure of the influenza virus NP polymers.
[Effect of the antiviral drug Ingaviruin on intracellular transformations and import into the nucleus of influenza A virus nucleocapsid protein].
It is shown that there is an association of tritium-labeled Ingavirin with the nuclear membranes of MDCK cells, and the investigations of the mechanisms of antiviral activity of Ingvirin promote the detection of potential targets to design novel antiviral agents.
Extracellular truncated influenza virus nucleoprotein.
[Antigenic variability of avian influenza virus A/H13, isolated in the USSR].
The antigenic structure of influenza H13 viruses isolated from wild birds in the USSR in 1976-1985 was studied and 2 replacements of arginine by lysine and asparagine by serine in positions 15 and 16 are the most significant.
Transient disulfide bonds formation in conformational maturation of influenza virus nucleocapsid protein (NP).
[Use of the plaque method to reveal the phenomenon of autointerference in influenza virus].
- N. Semenova, E. N. Kantorovich-Prokudina, I. A. Miasnikova, O. N. Berezina
- MedicineVoprosy virusologii
The paper describes a simple and convenient method for qualitative and quantitative evaluation of the capacity of influenza virus for autointerference consisting in the lack or considerable reduction…
Non-compact nucleocapsid protein multimers in influenza-virus-infected cells
It is demonstrated that, in addition to compact NP oligomers, incompletely folded NP multimers are detected intracellularly by SDS/PAGE carried out under weak dissociating conditions.