We generalize the concept of allostery from the traditional non active-site control of enzymes to virus maturation. Virtually all animal viruses transition from a procapsid, non infectious state, to a mature infectious state. The procapsid contains an encoded chemical program that is executed following an environmental cue. We developed an exceptionally accessible virus system for the study of the activators of maturation and the down stream consequences that result in particle stability and infectivity. Nudaurelia Capensis Omegavirus (NωV) is a T=4 icosahedral virus that undergoes a dramatic maturation in which the 490? spherical procapsid condenses to a 400? icosahedral shaped capsid with associated specific auto-proteolysis and stabilization. Employing X-ray crystallography, time resolved electron cryo-microscopy and hydrogen/deuterium exchange as well as biochemistry it was possible to define the mechanisms of allosteric communication among the 4 quasi-equivalent subunits in the icosahedral asymmetric unit. These gene products undergo proteolysis at different rates, dependent on quaternary structure environment, while particle stability is conferred globally following only a few local subunit transitions. We show that there is a close similarity between the concepts of tensegrity, associated with geodesic domes and mechanical engineering, and allostery, associated with biochemical control mechanisms.