Cell entry of BmCPV can be promoted by tyrosine-protein kinase Src64B-like protein

• Published in: Enzyme and microbial technology Vol. 121; pp. 1 - 7
• Main Authors: Zhang, Yiling, Zhu, Liyuan, Cao, Guangli, Sahib Zar, Mian, Hu, Xiaolong, Wei, Yuhong, Xue, Renyu, Gong, Chengliang
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.02.2019
• Subjects: BmCPV; Cell entry; Cellular signaling pathway; Src kinase; Src kinase; Cell entry; BmCPV; Cellular signaling pathway
• ISSN: 0141-0229; 1879-0909
• DOI: 10.1016/j.enzmictec.2018.10.012

•Function of tyrosine-protein kinase Src64B-like in the cell entry of BmCPV was investigated.•Silencing the expression of Src64B-like reduced the infection of BmCPV.•Overexpression of Src64B-like enhanced the infection of BmCPV.•BmCPV didn’t interact with Src64B-like protein directly in the infection process. Bombyx mori cytoplasmic polyhedrosis virus (BmCPV) is a non-enveloped dsRNA virus, which specifically infect the midgut epithelium of B. mori. BmCPV enters permissive cells via clathrin-dependent endocytosis employing β1 integrin mediated internalization. Until now, the cell entry mechanism of BmCPV has not been known clearly. Here, we investigated whether tyrosine-protein kinase Src64B-like is involved in the cell entry of BmCPV. The Src64B-like gene was cloned and expressed in Escherichia coli (E. coli), and the recombinant protein Src64B-like was used to immunize mouse for preparation of anti-Src64B-like polyclonal antibody (pAb). After Src64B-like gene was silenced by RNAi, the infection of BmCPV was reduced by 59.48% ± 2.18% and 92.22% ± 1.12% in vitro and in vivo autonomously. Contrary to it, BmCPV infection could be enhanced by increasing the expression of Src64B-like. In addition, immunofluorescence assay showed that Src64B-like protein did not co-localize with BmCPV in the cultured BmN cells during viral infection. These results indicate that Src64B-like protein participates and plays an important role in the cell entry of BmCPV, but not contacting directly with BmCPV.