The in situ structural characterization of the influenza A virus matrix M1 protein within a virion.
The first attempt has been made to suggest a model of influenza A virus matrix M1 protein spatial structure and molecule orientation within a virion on the basis of tritium planigraphy data and theoretical prediction results. Limited in situ proteolysis of the intact virions with bromelain and surface plasmon resonance spectroscopy study of the M1 protein interaction with lipid coated surfaces were used for independent confirmation of the proposed model.
Shishkov
Alexander V
AV
Department of Substance Structure, N.N. Semenov Institute of Chemical Physics, Russian Academy of Sciences, Moscow, Russia.
Bogacheva
Elena N
EN
Dolgov
Alexey A
AA
Chulichkov
Alexey L
AL
Knyazev
Denis G
DG
Fedorova
Natalia V
NV
Ksenofontov
Alexander L
AL
Kordyukova
Larisa V
LV
Lukashina
Elena V
EV
Mirsky
Vladimir M
VM
Baratova
Lyudmila A
LA
D001963:Bromelains / Q000378:metabolism; D018360:Crystallography, X-Ray; D006389:Hemagglutinins, Viral / Q000737:chemistry; D053122:Influenza A Virus, H3N2 Subtype / Q000737:chemistry*; D007553:Isotope Labeling; D007700:Kinetics; D008958:Models, Molecular; D020349:Surface Plasmon Resonance; D014316:Tritium; D014763:Viral Matrix Proteins / Q000737:chemistry*; D014771:Virion / Q000737:chemistry* / Q000378:metabolism
D006389:Hemagglutinins, Viral; C488936:M1 protein, Influenza A virus; D014763:Viral Matrix Proteins; D014316:Tritium; D001963:Bromelains