  Many viruses rely on the self-assembly of their capsids to protect and
transport their genomic material. For many viral systems, in particular for
human viruses like hepatitis B, adeno or human immunodeficiency virus, that
lead to persistent infections, capsomeres are continuously produced in the
cytoplasm of the host cell while completed capsids exit the cell for a new
round of infection. Here we use coarse-grained Brownian dynamics simulations of
a generic patchy particle model to elucidate the role of the dynamic supply of
capsomeres for the reversible self-assembly of empty T1 icosahedral virus
capsids. We find that for high rates of capsomere influx only a narrow range of
bond strengths exists for which a steady state of continuous capsid production
is possible. For bond strengths smaller and larger than this optimal value, the
reaction volume becomes crowded by small and large intermediates, respectively.
For lower rates of capsomere influx a broader range of bond strengths exists
for which a steady state of continuous capsid production is established,
although now the production rate of capsids is smaller. Thus our simulations
suggest that the importance of an optimal bond strength for viral capsid
assembly typical for in vitro conditions can be reduced by the dynamic influx
of capsomeres in a cellular environment.
