Rabbit haemorrhagic disease virus (RHDV) is used in Australia to control feral European rabbits that cause excessive damage to the agriculture and Australian ecosystems. Infected rabbits experience extremely rapid onset of liver failure, haemorrhages and death within 72 hours after infection. The virus belongs to the Caliciviridae family and contains a single-stranded RNA genome that encodes a capsid protein and several non-structural proteins. The functions of some of the non-structural proteins remain unknown, mostly due to the lack of a robust cell culture system. In order to elucidate functions of the uncharacterised proteins and better understand the infection process, we performed stable isotope labelling of amino acids in cell culture (SILAC) coupled with co-immunoprecipitations of the tagged proteins. This approach aimed at identification of cellular interaction partners of non-structural RHDV proteins in transiently transfected rabbit kidney cells. We found that one of the non-structural proteins, p23, binds chaperone proteins (heat shock proteins 70 and 110). This protein is also predicted to form a membrane-spanning channel which may disrupt ion balances and induce cellular stress. Our results allow to suggest that the heat shock proteins are involved in the stress response induced by p23. Another non-structural protein, the RNA-dependent RNA polymerase, which replicates viral genome, interacts with BRO1 domain-containing proteins. These proteins are involved in cellular membrane remodeling and cytoskeletal dynamics. This finding is in line with previous observations that the polymerase disrupts the Golgi architecture in a wide range of transfected cells, affecting normal cellular trafficking. Interactions between the BRO1 domain-containing proteins and the polymerase may facilitate the formation of the virus replication factories.