[Conditions of stability for the quaternary structure and antigenic activity of adenovirus hexon].
The procedure of SDS-PAGE was modified by lowering the temperature of protein sample dissociation to allow the separation of denaturated adenoviral hexon chains and native hexon capsomers (trimers) in the same gel. By combining the modified SDS-PAGE with dot and blot radioimmunoassays, the range of stability of the simian adenovirus SA7 hexon quaternary structure and its antigenicity was studied against a number of physical and chemical agents known to dissociate and denaturate proteins. A perfect correlation was found between the hexon native quaternary structure (trimer) and its immunoreactivity with anti-hexon immunoglobulins. The pattern of hexon trimer stability to a wide spectrum of denaturants suggests that its subunits are held together, mainly by hydrophobic interactions, in such a way that the innersubunit contact regions make up the "hydrophobic core" of the hexon molecule.
Grigor'ev
V G
VG
Khil'ko
S N
SN
Tikhonenko
T I
TI
D000256:Adenoviridae / Q000276:immunology*; D000260:Adenoviruses, Human / Q000032:analysis / Q000276:immunology*; D000261:Adenoviruses, Simian / Q000032:analysis / Q000276:immunology*; D000818:Animals; D000956:Antigens, Viral / Q000032:analysis*; D002213:Capsid / Q000032:analysis / Q000276:immunology*; D036022:Capsid Proteins; D002478:Cells, Cultured; D004589:Electrophoresis, Disc; D000939:Epitopes / Q000032:analysis*; D006801:Humans; D046911:Macromolecular Substances; D011489:Protein Denaturation; D013696:Temperature
D000956:Antigens, Viral; D036022:Capsid Proteins; D000939:Epitopes; D046911:Macromolecular Substances; C018315:hexon capsid protein, Adenovirus
Usloviia stabil'nosti chetvertichnoĭ struktury i antigennoĭ aktivnosti geksona adenovirusov.