Identification of a novel host protein interacting with the structural protein VP2 of deformed wing virus by yeast two-hybrid screening

Huang, Sichao; Fei, Dongliang; Ma, Yueyu; Wang, Chen; Shi, Donghui; Liu, Kunyang; Li, Ming; Ma, Mai‐Juan

doi:10.1016/j.virusres.2020.198072

Cited by 1 publication

(1 citation statement)

References 47 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The bees were placed on ice and anesthetized with CO 2 for 1 min. Group I was injected with 1 μL of a DWV suspension between the 2nd and 3rd integuments using a similar controlled-volume syringe ( Huang et al, 2020 ), and group II was injected with 1 μL PBS as control. The inoculated bees were fed with sufficient sterilized food and water.…”

Section: Methodsmentioning

confidence: 99%

Interaction between the VP2 protein of deformed wing virus and host snapin protein and its effect on viral replication

Sun¹,

Li²,

Ma³

et al. 2023

Front. Microbiol.

Self Cite

View full text Add to dashboard Cite

IntroductionDeformed wing virus (DWV) is one of the causative agents of colony collapse disorder. The structural protein of DWV plays a vital role in the process of viral invasion and host infection; however, there is limited research on DWV.Methods and ResultsIn this study, we screened the host protein snapin, which can interact with the VP2 protein of DWV, using the yeast two-hybrid system. Through computer simulation and GST pull-down and CO-IP assays, an interaction between snapin and VP2 was confirmed. Furthermore, immunofluorescence and co-localization experiments revealed that VP2 and snapin primarily co-localized in the cytoplasm. Consequently, RNAi was used to interfere with the expression of snapin in worker bees to examine the replication of DWV after the interference. After silencing of snapin, the replication of DWV in worker bees was significantly downregulated. Hence, we speculated that snapin was associated with DWV infection and involved in at least one stage of the viral life cycle. Finally, we used an online server to predict the interaction domains between VP2 and snapin, and the results indicate that the interaction domain of VP2 was approximately located at 56–90, 136–145, 184–190, and 239–242 aa and the snapin interaction domain was approximately located at 31–54 and 115–136 aa.ConclusionThis research confirmed that DWV VP2 protein could interacts with the snapin of host protein, which provides a theoretical basis for further investigation of its pathogenesis and development of targeted therapeutic drugs.

show abstract

Section: Methodsmentioning

confidence: 99%