The presented data are also in agreement with the function of eEF1A as a chaperone of the viral RdRp. Binding between the eEF1A and RdRp might alter the structure of the RdRp that favors de novo initiation for RNA synthesis. Indeed, the chaperone activity of eEF1A and its bacterial homolog EF-Tu has been shown before [66, 67] . Moreover, the EF-Tu-EF-Ts complex is thought to function in the Qbeta replicase complex as a chaperone for maintaining the active conformation of the RdRp protein [68] .