It is a lytic phage, though under certain circumstances has been observed to display a delay in lysis which may be described as a "carrier state".

Fusion of the viral envelope with the bacterial outer membrane is facilitated by the phage protein, P6.

A copy of the sense strand of the large genome segment (6374 bases) is then synthesized (transcription) on the vertices of the capsid, with the RNA-dependent RNA polymerase, P2, and released into the host cell cytosol.

The completed phage progeny remain in the cytosol until sufficient levels of the lytic protein P5 degrade the host cell wall.

The crystal structure of the Φ6 polymerase, solved in complex with a number of ligands, provides insights towards understanding the mechanism of primer-independent initiation of RNA-dependent RNA polymerization.

The purified Φ6 RdRP displays processive elongation in vitro and self-assembles along with polymerase complex proteins into subviral particles that are fully functional.

[5] Φ6 has been studied as a model to understand how segmented RNA viruses package their genomes, its structure has been studied by scientists interested in lipid-containing bacteriophages, and it has been used as a model organism to test evolutionary theory such as Muller's ratchet.