While SDS-PAGE/immunoblotting is a valuable approach for the character
ization of monoclonal antibodies, the denaturing conditions involved c
an compromise the recognition of conformational epitopes. This report
demonstrates that a group specific epitope on adenovirus hexon can be
recognized by immunoblotting following SDS-PAGE provided that samples
are not boiled prior to electrophoresis. Under these conditions, multi
ple bands corresponding to native forms of heron were detected above t
he position of the denatured hexon monomer. Among representative serot
ypes of subgroups A, B and F, two predominant bands, corresponding to
hexon trimers and 'group of nine' herons (GONs), were routinely observ
ed. In contrast, higher order structures, in addition to trimers and G
ONs, were characteristic of subgroup C adenoviruses. These serotypic d
ifferences in stability of hexon structures may reflect differences in
protein-protein interactions within the corresponding virions.