Identification of protein interactions of grapevine fanleaf virus RNA-dependent RNA polymerase during infection of by affinity purification and tandem mass spectrometry.

Osterbaan, Larissa J, Hoyle, Victoria, Curtis, Michelle, DeBlasio, Stacy, Rivera, Keith D, Heck, Michelle, Fuchs, Marc (May 2021) Identification of protein interactions of grapevine fanleaf virus RNA-dependent RNA polymerase during infection of by affinity purification and tandem mass spectrometry. The Journal of general virology, 102 (5). ISSN 1465-2099

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Abstract

The RNA-dependent RNA polymerase (1E) is involved in replication of grapevine fanleaf virus (GFLV, , ) and causes vein clearing symptoms in . Information on protein 1E interaction with other viral and host proteins is scarce. To study protein 1E biology, three GFLV infectious clones, i.e. GHu (a symptomatic wild-type strain), GHu-1E (an asymptomatic GHu mutant) and F13 (an asymptomatic wild-type strain), were engineered with protein 1E fused to a V5 epitope tag at the C-terminus. Following -mediated delivery of GFLV clones in and protein extraction at seven dpi, when optimal 1E:V5 accumulation was detected, two viral and six plant putative interaction partners of V5-tagged protein 1E were identified for the three GFLV clones by affinity purification and tandem mass spectrometry. This study provides insights into the protein interactome of 1E during GFLV systemic infection in and lays the foundation for validation work.

Item Type: Paper
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > RNA polymerase
organism description > plant
biotechnology > chromatography > protein purification
CSHL Authors:
Communities: CSHL labs > Pappin lab
Depositing User: Sasha Luks-Morgan
Date: 27 May 2021
Date Deposited: 24 Jun 2021 13:19
Last Modified: 29 Jul 2021 13:16
PMCID: PMC8295916
URI: https://repository.cshl.edu/id/eprint/40225

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