Abstract
Virus-like particles (VLPs) find applications across many different fields, aided by their stability, capacity for large-scale production, and presumed structural homogeneity. These attributes are a result of their highly efficient self-assembly, which stems from the evolutionary pressures on the natural viruses from which they are derived. It is found that VLPs based on the Leviphage PP7 assemble in an unexpectedly wide range of morphologies. The relative abundance of these structures is sensitive to small changes in the coat protein sequence. These results raise the possibility that structural plasticity may be a general property of such self-assembling structures rather than an exception.