The emerging picture on the functions of eEF1Bc and eEF1A is that these translation elongation factors play different, yet complementary roles in TBSV replication as suggested in Figure 9B . While eEF1Bc binds to SL1, eEF1A has been shown to bind to both p92 pol RdRp and the SL3 region of TBSV (+)repRNA [23, 24] . The binding of the RNA by eEF1Bc promotes the opening of the closed 39-terminal structure, whereas eEF1A facilitates the proper and efficient binding of the RdRp to the 39 terminal RSE sequence of the viral RNA, which is required for the assembly of the viral replicase complex [11, 39] , prior to initiation of (-)-strand synthesis (Figure 9 ) [23, 24] . The binding of eEF1A-RdRp complex to the RSE might lead to proper positioning of the RdRp over the 39-terminal gPR promoter sequence opened up by eEF1Bc, thus facilitating the initiation of (-)RNA synthesis starting from the 39-terminal cytosine ( Figure 9B) . Altogether, the two translation factors facilitate the efficient initiation of (-)-strand synthesis in addition to reducing the possibility of re-utilization of the (+)-strand template for additional rounds of (-)-strand synthesis. This regulation of RNA synthesis by the co-opted host factors shows the specialized use of host components to serve the need of viral replication.