Biology Reference
In-Depth Information
Fig. 6.
Superimposed representations of components of the double-shelled
structure around an icosahedral three-fold axis. Five icosahedrally unique P8-
trimers sit on different environments on the surface of the core particle. Spaces
between inner core proteins are well covered by outer P8-trimers.
surface of the core. When we examine the structure of RDV in this
context, we see that the edges of the P8-trimer are not parallel to the
line that can be drawn between adjacent icosahedral five-fold axes
(Fig. 6). This discrepancy suggests the absence of any regular corre-
spondence between the core proteins and the outer capsid proteins,
which might result, for example, in a T
9 structure. This structural
feature would determine subsequent binding of P8-trimers and result
in a T
=
13 structure, which has been hard to interpret, particularly
from a biochemical perspective, because some of the P8-trimers should
span the margins of icosahedral particles.
Biochemical evidence to support of the mechanism of assembly of
double-layered capsids with disparate icosahedral lattices, as described
above, was obtained from studies of chimeric virus-like particles with
components derived from different viral strains, which allowed dis-
crimination among the respective proteins in assembled particles either
=
