Comparative study of the hexons in adenoviruses of the genus Mastadenovirus
Kovalishin, G.G.; Vantsak, N.P.; Diachenko, N.S.; Kiseleva, E.K.; Zhovnovataia, V.L.
Mikrobiolohichnyi Zhurnal 48(2): 50-55
1986
ISSN/ISBN: 0201-8462 PMID: 2478865 Document Number: 273932
The method of disc-electrophoresis in SDS (sodium dodecyl sulphate)-PAAG was used for a comparative study of structural hexons of human adenoviruses of the 1st, 6th and 10th species and of simian adenoviruses of the 16th species. Variations are found in the molecular weight of hexon polypeptides of human adenoviruses (Ad h1-119.5 kDalton, Ad h6-124 kDalton, Ad h10-119.2 kDalton) and simian ones (Ad sim16-113.2 kDalton) differing in the biological properties. The data obtained indicate that the electrophoretic mobility of polypeptides of the major capsid protein of adenoviruses in SDS-PAAG and its molecular weight are strictly individual characteristic of each adenovirus. Spontaneous splitting of the fragment of hexon polypeptide with the molecular weight of 16 kDalton is established to occur in preparations of Ad h1 under conditions of long storage. Hexone polypeptide with molecular weight of 103.4 kDalton is stable and retains both the genus-, subgenus-specific determinants and the species-specific determinant stipulating the species uniqueness of the adenoviruses.