The DOI matches its Crossref record; 37 of the 37 references it cites were found in a registry or an index.
Coronavirus NSP6 restricts autophagosome expansion
Open accessAbstract
Autophagy is a cellular response to starvation that generates autophagosomes to carry long-lived proteins and cellular organelles to lysosomes for degradation. Activation of autophagy by viruses can provide an innate defense against infection, and for (+) strand RNA viruses autophagosomes can facilitate assembly of replicase proteins. We demonstrated that nonstructural protein (NSP) 6 of the avian coronavirus, infectious bronchitis virus (IBV), generates autophagosomes from the ER. A statistical analysis of MAP1LC3B puncta showed that NSP6 induced greater numbers of autophagosomes per cell compared with starvation, but the autophagosomes induced by NSP6 had smaller diameters compared with starvation controls. Small diameter autophagosomes were also induced by infection of cells with IBV, and by NSP6 proteins of MHV and SARS and NSP5, NSP6, and NSP7 of arterivirus PRRSV. Analysis of WIPI2 puncta induced by NSP6 suggests that NSP6 limits autophagosome diameter at the point of omegasome formation. IBV NSP6 also limited autophagosome and omegasome expansion in response to starvation and Torin1 and could therefore limit the size of autophagosomes induced following inhibition of MTOR signaling, as well as those induced independently by the NSP6 protein itself. MAP1LC3B-puncta induced by NSP6 contained SQSTM1, which suggests they can incorporate autophagy cargos. However, NSP6 inhibited the autophagosome/lysosome expansion normally seen following starvation. Taken together the results show that coronavirus NSP6 proteins limit autophagosome expansion, whether they are induced directly by the NSP6 protein, or indirectly by starvation or chemical inhibition of MTOR signaling. This may favor coronavirus infection by compromising the ability of autophagosomes to deliver viral components to lysosomes for degradation.
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Autophagosome formation: core machinery and adaptations
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Autophagosomes form at ER–mitochondria contact sites
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Termination of autophagy and reformation of lysosomes regulated by mTOR
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Coronavirus avian infectious bronchitis virus
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HSV-1 ICP34.5 Confers Neurovirulence by Targeting the Beclin 1 Autophagy Protein
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Subversion of Cellular Autophagosomal Machinery by RNA Viruses
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Human Coronavirus: Host-Pathogen Interaction
Fung, T. S., & Liu, D. X. (2019) · Annual Review of Microbiology · doi:10.1146/annurev-micro-020518-115759 · Cited by 960
Autophagy in inflammation, infection, and immunometabolism
Deretic, V. (2021) · Immunity · doi:10.1016/j.immuni.2021.01.018 · Cited by 862
Multilevel proteomics reveals host perturbations by SARS-CoV-2 and SARS-CoV
Stukalov, A., Girault, V., Grass, V., Karayel, O., Bergant, V., Urban, C., Haas, D. A., Huang, Y., Oubraham, L., Wang, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03493-4 · Cited by 685
Yoshimoto, F. K. (2020) · The Protein Journal · doi:10.1007/s10930-020-09901-4 · Cited by 543
Role of Structural and Non-Structural Proteins and Therapeutic Targets of SARS-CoV-2 for COVID-19
Yadav, R., Chaudhary, J. K., Jain, N., Chaudhary, P. K., Khanra, S., Dhamija, P., Sharma, A., Kumar, A., & Handu, S. (2021) · Cells · doi:10.3390/cells10040821 · Cited by 451
Metadata
- Authors
- Cottam, E. M., Whelband, M. C., & Wileman, T.
- Venue
- Autophagy
- Publisher
- Informa UK Limited
- Published
- 2014-06-11
- Volume
- 10
- Issue
- 8
- Pages
- 1426-1441
- ISSN
- 1554-8627 (ISSN-L)
- 1554-8635
- OpenAlex
- W1985360059
- Cited by
- 291
- References
- 37
- FWCI
- 2.70
- Type
- journal article
- Language
- en
- Open access
- hybrid
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