Associated diseases include chronic diarrhoea and pale blue iridescence in the guts of larvae.

They exhibit striking capsid stability, which is fully capable of endogenous RNA transcription and processing.

The overall folds of cypovirus proteins are similar to those of other reoviruses, but they have insertional domains and unique structures that contribute to their extensive intermolecular interactions.

The cypovirus turret protein contains two methylase domains with a highly conserved helix-pair/β-sheet/helix-pair sandwich fold, but lacks the β-barrel flap present in orthoreovirus λ2.

These dissolve in its digestive tract, releasing the virus particles that penetrate the gut epithelial cells.