Cell entry of BmCPV can be promoted by tyrosine-protein kinase Src64B-like protein
•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 infectio...
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Published in | Enzyme and microbial technology Vol. 121; pp. 1 - 7 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
01.02.2019
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Subjects | |
Online Access | Get full text |
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Summary: | •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. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0141-0229 1879-0909 |
DOI: | 10.1016/j.enzmictec.2018.10.012 |