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SNAP47 Interacts with ATG14 to Promote VP1 Conjugation and CVB3 Propagation Xiang, Pinhao; Mohamud, Yasir; Luo, Honglin

Abstract

Coxsackievirus B3 (CVB3), an enterovirus (EV) in the family of Picornaviridae, is a global human pathogen for which effective antiviral treatments and vaccines are lacking. Previous research demonstrated that EV-D68 downregulated the membrane fusion protein SNAP47 (synaptosome associated protein 47) and SNAP47 promoted EV-D68 replication via regulating autophagy. In the current study, we investigated the interplay between CVB3 and cellular SNAP47 using HEK293T/HeLa cell models. We showed that, upon CVB3 infection, protein levels of SNAP47 decreased independent of the activity of virus-encoded proteinase 3C. We further demonstrated that the depletion of SNAP47 inhibited CVB3 infection, indicating a pro-viral function of SNAP47. Moreover, we found that SNAP47 co-localizes with the autophagy-related protein ATG14 on the cellular membrane fractions together with viral capsid protein VP1, and expression of SNAP47 or ATG14 enhanced VP1 conjugation. Finally, we revealed that disulfide interactions had an important role in strengthening VP1 conjugation. Collectively, our study elucidated a mechanism by which SNAP47 and ATG14 promoted CVB3 propagation through facilitating viral capsid assembly.

Item Metadata

Title
SNAP47 Interacts with ATG14 to Promote VP1 Conjugation and CVB3 Propagation
Creator
Xiang, Pinhao; Mohamud, Yasir; Luo, Honglin
Contributor
University of British Columbia. Centre for Heart Lung Innovation; St. Paul's Hospital (Vancouver, B.C.)
Publisher
Multidisciplinary Digital Publishing Institute
Date Issued
2021-08-20
Description
Coxsackievirus B3 (CVB3), an enterovirus (EV) in the family of Picornaviridae, is a global human pathogen for which effective antiviral treatments and vaccines are lacking. Previous research demonstrated that EV-D68 downregulated the membrane fusion protein SNAP47 (synaptosome associated protein 47) and SNAP47 promoted EV-D68 replication via regulating autophagy. In the current study, we investigated the interplay between CVB3 and cellular SNAP47 using HEK293T/HeLa cell models. We showed that, upon CVB3 infection, protein levels of SNAP47 decreased independent of the activity of virus-encoded proteinase 3C. We further demonstrated that the depletion of SNAP47 inhibited CVB3 infection, indicating a pro-viral function of SNAP47. Moreover, we found that SNAP47 co-localizes with the autophagy-related protein ATG14 on the cellular membrane fractions together with viral capsid protein VP1, and expression of SNAP47 or ATG14 enhanced VP1 conjugation. Finally, we revealed that disulfide interactions had an important role in strengthening VP1 conjugation. Collectively, our study elucidated a mechanism by which SNAP47 and ATG14 promoted CVB3 propagation through facilitating viral capsid assembly.
Subject
SNARE; SNAP47; ATG14; autophagy; coxsackievirus B3; VP1
Genre
Article
Type
Text
Language
eng
Date Available
2021-09-03
Provider
Vancouver : University of British Columbia Library
Rights
CC BY 4.0
DOI
10.14288/1.0401907
URI
http://hdl.handle.net/2429/79639
Affiliation
Medicine, Faculty of; Other UBC; Medicine, Department of; Pathology and Laboratory Medicine, Department of
Citation
Cells 10 (8): 2141 (2021)
Publisher DOI
10.3390/cells10082141
Peer Review Status
Reviewed
Scholarly Level
Faculty; Researcher
Rights URI
https://creativecommons.org/licenses/by/4.0/
Aggregated Source Repository
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CC BY 4.0