Although previous works showed that SYK accumulated in the cytoplasm in RB cells (Zhang et al. 2012), our immunofluorescent staining results showed SYK expression on the cell surface. SYK protein localization on the cell membrane facilitates activated CTLs to specifically recognize the antigens present on the surface of RB-Y79 cells. This is key for specific lymphocyte-based immunotherapy. SYK is also a member of a family of cytoplasmic non-receptor tyrosine kinases. This confers an additional advantage for its use in targeted cell immunotherapy because RB-Y79 cells express the SYK protein on the cell surface, allowing it to be recognized by cytotoxic immune cells, while hematopoietic cells, which express cytoplasmic SYK, may be protected from SYK-driven immune cytotoxic activity (Chauhan et al. 2016). Although we demonstrated SYK gene expression in SYK-DCs by qRT-PCR, we failed to detect SYK protein on the surface of infected DC cells using flow cytometry (data not shown). The possible reasons why we failed to detect the SYK signal in DCs could due to two aspects. Firstly, in a classical pathway in DCs, the antigen is cleaved into peptides by endosomal proteases, particularly cathepsin S, and bound by class I molecules probably in the endocytic compartment itself (Rock and Shen 2005). Secondly, the processed antigen could not be presented everlastingly on the DC surface, published **data** have also explained how duration of antigen presentation affects the dynamics of T-cell-DC interactions and consequently determine immune response (Benson et al. 2015). Thus, it is easy to understand why we see no staining for SYK on the pulsed DCs.