Mutual spatial orientation of hexons in the adenovirus capsid by electron microscopy and modelling.
On the basis of electron microscopic analysis of the virion and model experiments there are four hexon species in the adenovirus capsid which have different positional status and spatial orientation as compared to the six nearest neighbouring capsomers. The binding pattern of the polypeptide subunits according to their orientation is also different. The four hexon species are situated beside one another in the capsid and they form the capsid of 240 hexons besides the penton by repeating symmetrically 60 times, as a group of four hexons (GOF). Electron microscopic analysis and model experiments lead to the conclusion that the mutual spatial orientation of GOF hexons can be parallel (their longitudinal axes are parallel), or the direction of their longitudinal axes is different in one or two planes, thus they form different angles with the longitudinal axes of the neighbouring hexons. In the latter cases therefore, a bend and torsion of the bindings (connective elements) can be supposed as compared to the tendency-plane of parallel bindings. Based on the different combinations of the three kinds of rotational orientation of polypeptide subunits and of the different spatial orientation of hexons, six kinds of interhexonal bindings can be found in the adenovirus capsid. The distribution and characteristics of the 690 interhexonal bindings are the following; 240 bindings of "one-to-two" polypeptide orientation with parallel spatial orientation; 180 bindings of "one-to-two" polypeptide with spatial orientation divergent in two planes; 30 bindings of "one-to-one" polypeptide orientation with parallel spatial orientation; 60 bindings of "one-to-one" polypeptide orientation with spatial orientations divergent in one plane; 60 bindings of "one-to-one" polypeptide orientation with spatial orientation divergent in two planes; 120 bindings of "two-to-two" polypeptide orientation with spatial orientation divergent in two planes. The dissociational sequence of the capsid suggests that the firmest bindings are the ones having "one-to-two" polypeptide orientation and parallel spatial orientation. It may be supposed that any two hexons are able to connect to each other according to all three polypeptide orientations and the connections can tolerate the bends and torsions arising from the icosahedral structure. This suggests that only one kind of hexon is existing and the adenovirus capsid is formed by a homogeneous hexon population.
D000256:Adenoviridae / Q000648:ultrastructure*; D002213:Capsid / Q000032:analysis*; D008854:Microscopy, Electron / Q000379:methods; D008958:Models, Molecular; D011487:Protein Conformation; D014771:Virion / Q000648:ultrastructure*