PMID- 30482152
OWN - NLM
STAT- MEDLINE
DCOM- 20181211
LR  - 20181211
IS  - 1608-3040 (Electronic)
IS  - 0006-2979 (Linking)
VI  - 83
IP  - 11
DP  - 2018 Nov
TI  - Aggregation of Influenza A Virus Nuclear Export Protein.
PG  - 1411-1421
LID - 10.1134/S0006297918110111 [doi]
AB  - 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.
FAU - Golovko, A O
AU  - Golovko AO
AD  - Lomonosov Moscow State University, Department of Bioengineering and 
      Bioinformatics, Moscow, 119991, Russia. nastiagolovko@mail.ru.
FAU - Koroleva, O N
AU  - Koroleva ON
AD  - Lomonosov Moscow State University, Department of Chemistry, Moscow, 119991, 
      Russia. koroleva@genebee.msu.ru.
FAU - Tolstova, A P
AU  - Tolstova AP
AD  - Lomonosov Moscow State University, Department of Physics, Moscow, 119991, Russia. 
      tolstova@physics.msu.ru.
FAU - Kuz'mina, N V
AU  - Kuz'mina NV
AD  - Lomonosov Moscow State University, Department of Biology, Moscow, 119991, Russia. 
      kuzmina-natasha@inbox.ru.
AD  - Frumkin Institute of Physical Chemistry and Electrochemistry, Russian Academy of 
      Sciences, Moscow, 119071, Russia.
FAU - Dubrovin, E V
AU  - Dubrovin EV
AD  - Lomonosov Moscow State University, Department of Physics, Moscow, 119991, Russia. 
      dubrovin@polly.phys.msu.ru.
FAU - Drutsa, V L
AU  - Drutsa VL
AD  - Lomonosov Moscow State University, Belozersky Research Institute of 
      Physico-Chemical Biology, Moscow, 119991, Russia. drutsa@genebee.msu.ru.
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Biochemistry (Mosc)
JT  - Biochemistry. Biokhimiia
JID - 0376536
RN  - 0 (Multiprotein Complexes)
RN  - 0 (Protein Aggregates)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Viral Proteins)
SB  - IM
MH  - Influenza A Virus, H1N1 Subtype/*chemistry/genetics/metabolism
MH  - Multiprotein Complexes/*chemistry/genetics/metabolism
MH  - *Protein Aggregates
MH  - Recombinant Proteins/chemistry/genetics/metabolism
MH  - Viral Proteins/*chemistry/genetics/metabolism
EDAT- 2018/11/30 06:00
MHDA- 2018/12/12 06:00
CRDT- 2018/11/29 06:00
PHST- 2018/11/29 06:00 [entrez]
PHST- 2018/11/30 06:00 [pubmed]
PHST- 2018/12/12 06:00 [medline]
AID - BCM83111746 [pii]
AID - 10.1134/S0006297918110111 [doi]
PST - ppublish
SO  - Biochemistry (Mosc). 2018 Nov;83(11):1411-1421. doi: 10.1134/S0006297918110111.