Chikungunya virus non-structural protein nsP3 interacts with Aedes aegypti DEAD-box helicase RM62F

Simple item page
dc.contributor.authorKumar, Ramesh
dc.contributor.authorKaur, Inderjeet
dc.contributor.authorChattopadhyay, Soma
dc.contributor.authorNayak, Debasis
dc.contributor.authorMathur, Kalika
dc.date.accessioned2023-05-01T17:47:56Z
dc.date.available2023-05-01T17:47:56Z
dc.date.issued2021
dc.description.abstractThe non-structural proteins (nsPs) of the chikungunya virus (CHIKV) form the virus’s replication complex. They are known to participate in several functions that allow efficient replication of the virus in diverse host systems. One such function is evading the host defense system such as RNA interference (RNAi). Two nsPs of CHIKV, namely, nsP2 and nsP3, were found to suppress the host/vector RNAi machinery and exhibit RNAi suppressor activity. The present study was undertaken to identify interacting partners of CHIKV-nsP3 in Aedes aegypti. We performed pull-down assays with the mass spectrometry approach and showed the interaction of CHIKV-nsP3 with several Aedes proteins. Further co-immunoprecipitation assays revealed that CHIKV-nsP3 interacts with RM62F, a DEAD-box containing RNA known to play roles in multiple gene regulatory processes such as alternative splicing, RNA release, and also is a component of Ago2-RISC complex.en_US
dc.identifier.urihttp://hdl.handle.net/123456789/1058
dc.language.isoenen_US
dc.publisherVirus Diseaseen_US
dc.subjectChikungunya virus Aedes aegypti nsP3 RNA interference Arbovirusesen_US
dc.titleChikungunya virus non-structural protein nsP3 interacts with Aedes aegypti DEAD-box helicase RM62Fen_US
dc.typeArticleen_US
Files
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
Chikungunya virus non-structural proteinnsP3 interacts with Aedes aegypti DEAD-boxhelicase RM62F.pdf
Size:
692.49 KB
Format:
Adobe Portable Document Format
Description:
Download
License bundle
Now showing 1 - 1 of 1
No Thumbnail Available
Name:
license.txt
Size:
1.71 KB
Format:
Item-specific license agreed upon to submission
Description:
Download
Collections
School of Interdisciplinary & Applied Sciences