Known host-parasite molecular interactions are widespread among parasite families, but these interactions have to be particularly large considering the viruses which generally encode for few proteins. Since some particular virus-host interactions are well described, no global study yet showed multiple and simultaneous interactions in a host-parasite biological system. To prove that these multiple interactions occur in biological conditions, the complexes formed by a plant virus (Rice Yellow Mottle Virus) and the proteins of its natural host (rice) were extracted and purified from infected tissue sample. Remarkably, mass spectrometry permitted to identify a large number of proteins from the complexes which are involved in different functions not encoded by the virus but probably essential for its biological life cycle. This proteinic recruiting was strongly confirmed by the repetition of experiments using different pairs of virus-host, and the use of high salt concentration to extract the complexes. We mainly identified proteins involved in plant defense, in metabolism, translation and protein synthesis and some proteins involved in transport. This study demonstrates that viruses are able to recruit many proteins from their hosts to ensure their development. Among different pairs of virus-host, similar proteins functions were identified suggesting a particular importance of these proteins for viruses. The identification of particular paralog proteins among multigenic families suggests the high specificity of the recruiting for some protein functions.