ORF3a of the COVID-19 virus SARS-CoV-2 blocks HOPS complex-mediated assembly of the SNARE complex required for autolysosome formation

Autophagy acts as a cellular surveillance mechanism to combat invading pathogens. Viruses have evolved various strategies to block autophagy and even subvert it for their replication and release. Here, we demonstrated that ORF3a of the COVID-19 virus SARS-CoV-2 inhibits autophagy activity by blockin...

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Published inDevelopmental cell Vol. 56; no. 4; pp. 427 - 442.e5
Main Authors Miao, Guangyan, Zhao, Hongyu, Li, Yan, Ji, Mingming, Chen, Yong, Shi, Yi, Bi, Yuhai, Wang, Peihui, Zhang, Hong
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 22.02.2021
Subjects
Autophagosomes - metabolism
Autophagy
Autophagy-Related Proteins - metabolism
COVID-19
COVID-19 - metabolism
COVID-19 - virology
DMV
HEK293 Cells
HeLa Cells
HOPS
Humans
Lysosomes - metabolism
ORF3a
Protein Binding
SARS-CoV-2
SARS-CoV-2 - metabolism
SARS-CoV-2 - pathogenicity
SNARE
SNARE Proteins - metabolism
Vesicular Transport Proteins - metabolism
Viroporin Proteins - genetics
Viroporin Proteins - metabolism
COVID-19
SARS-CoV-2
autophagy
HOPS
DMV
ORF3a
SNARE
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Abstract Autophagy acts as a cellular surveillance mechanism to combat invading pathogens. Viruses have evolved various strategies to block autophagy and even subvert it for their replication and release. Here, we demonstrated that ORF3a of the COVID-19 virus SARS-CoV-2 inhibits autophagy activity by blocking fusion of autophagosomes/amphisomes with lysosomes. The late endosome-localized ORF3a directly interacts with and sequestrates the homotypic fusion and protein sorting (HOPS) component VPS39, thereby preventing HOPS complex from interacting with the autophagosomal SNARE protein STX17. This blocks assembly of the STX17-SNAP29-VAMP8 SNARE complex, which mediates autophagosome/amphisome fusion with lysosomes. Expression of ORF3a also damages lysosomes and impairs their function. SARS-CoV-2 virus infection blocks autophagy, resulting in accumulation of autophagosomes/amphisomes, and causes late endosomal sequestration of VPS39. Surprisingly, ORF3a from the SARS virus SARS-CoV fails to interact with HOPS or block autophagy. Our study reveals a mechanism by which SARS-CoV-2 evades lysosomal destruction and provides insights for developing new strategies to treat COVID-19. [Display omitted] •SARS-CoV-2 virus infection or expression of ORF3a blocks formation of autolysosomes•SARS-CoV-2 ORF3a sequestrates the HOPS component VPS39 on late endosomes•SARS-CoV-2 ORF3a impairs the assembly of the STX17-SNAP29-VAMP8 SNARE complex•SARS virus ORF3a fails to interact with VPS39 or affect autophagy activity Miao et al. demonstrate that late endosome-localized ORF3a of the COVID-19 virus SARS-CoV-2 sequestrates the HOPS component VPS39. ORF3a blocks autophagosome/amphisome fusion with lysosomes by preventing the assembly of the STX17-SNAP29-VAMP8 SNARE complex. SARS-CoV-2-infected cells also exhibit a defect in autophagosome maturation and sequestration of VPS39 on late endosomes.
AbstractList Autophagy acts as a cellular surveillance mechanism to combat invading pathogens. Viruses have evolved various strategies to block autophagy and even subvert it for their replication and release. Here, we demonstrated that ORF3a of the COVID-19 virus SARS-CoV-2 inhibits autophagy activity by blocking fusion of autophagosomes/amphisomes with lysosomes. The late endosome-localized ORF3a directly interacts with and sequestrates the homotypic fusion and protein sorting (HOPS) component VPS39, thereby preventing HOPS complex from interacting with the autophagosomal SNARE protein STX17. This blocks assembly of the STX17-SNAP29-VAMP8 SNARE complex, which mediates autophagosome/amphisome fusion with lysosomes. Expression of ORF3a also damages lysosomes and impairs their function. SARS-CoV-2 virus infection blocks autophagy, resulting in accumulation of autophagosomes/amphisomes, and causes late endosomal sequestration of VPS39. Surprisingly, ORF3a from the SARS virus SARS-CoV fails to interact with HOPS or block autophagy. Our study reveals a mechanism by which SARS-CoV-2 evades lysosomal destruction and provides insights for developing new strategies to treat COVID-19.Autophagy acts as a cellular surveillance mechanism to combat invading pathogens. Viruses have evolved various strategies to block autophagy and even subvert it for their replication and release. Here, we demonstrated that ORF3a of the COVID-19 virus SARS-CoV-2 inhibits autophagy activity by blocking fusion of autophagosomes/amphisomes with lysosomes. The late endosome-localized ORF3a directly interacts with and sequestrates the homotypic fusion and protein sorting (HOPS) component VPS39, thereby preventing HOPS complex from interacting with the autophagosomal SNARE protein STX17. This blocks assembly of the STX17-SNAP29-VAMP8 SNARE complex, which mediates autophagosome/amphisome fusion with lysosomes. Expression of ORF3a also damages lysosomes and impairs their function. SARS-CoV-2 virus infection blocks autophagy, resulting in accumulation of autophagosomes/amphisomes, and causes late endosomal sequestration of VPS39. Surprisingly, ORF3a from the SARS virus SARS-CoV fails to interact with HOPS or block autophagy. Our study reveals a mechanism by which SARS-CoV-2 evades lysosomal destruction and provides insights for developing new strategies to treat COVID-19.
Autophagy acts as a cellular surveillance mechanism to combat invading pathogens. Viruses have evolved various strategies to block autophagy and even subvert it for their replication and release. Here, we demonstrated that ORF3a of the COVID-19 virus SARS-CoV-2 inhibits autophagy activity by blocking fusion of autophagosomes/amphisomes with lysosomes. The late endosome-localized ORF3a directly interacts with and sequestrates the homotypic fusion and protein sorting (HOPS) component VPS39, thereby preventing HOPS complex from interacting with the autophagosomal SNARE protein STX17. This blocks assembly of the STX17-SNAP29-VAMP8 SNARE complex, which mediates autophagosome/amphisome fusion with lysosomes. Expression of ORF3a also damages lysosomes and impairs their function. SARS-CoV-2 virus infection blocks autophagy, resulting in accumulation of autophagosomes/amphisomes, and causes late endosomal sequestration of VPS39. Surprisingly, ORF3a from the SARS virus SARS-CoV fails to interact with HOPS or block autophagy. Our study reveals a mechanism by which SARS-CoV-2 evades lysosomal destruction and provides insights for developing new strategies to treat COVID-19. Miao et al. demonstrate that late endosome-localized ORF3a of the COVID-19 virus SARS-CoV-2 sequestrates the HOPS component VPS39. ORF3a blocks autophagosome/amphisome fusion with lysosomes by preventing the assembly of the STX17-SNAP29-VAMP8 SNARE complex. SARS-CoV-2-infected cells also exhibit a defect in autophagosome maturation and sequestration of VPS39 on late endosomes.
Autophagy acts as a cellular surveillance mechanism to combat invading pathogens. Viruses have evolved various strategies to block autophagy and even subvert it for their replication and release. Here, we demonstrated that ORF3a of the COVID-19 virus SARS-CoV-2 inhibits autophagy activity by blocking fusion of autophagosomes/amphisomes with lysosomes. The late endosome-localized ORF3a directly interacts with and sequestrates the homotypic fusion and protein sorting (HOPS) component VPS39, thereby preventing HOPS complex from interacting with the autophagosomal SNARE protein STX17. This blocks assembly of the STX17-SNAP29-VAMP8 SNARE complex, which mediates autophagosome/amphisome fusion with lysosomes. Expression of ORF3a also damages lysosomes and impairs their function. SARS-CoV-2 virus infection blocks autophagy, resulting in accumulation of autophagosomes/amphisomes, and causes late endosomal sequestration of VPS39. Surprisingly, ORF3a from the SARS virus SARS-CoV fails to interact with HOPS or block autophagy. Our study reveals a mechanism by which SARS-CoV-2 evades lysosomal destruction and provides insights for developing new strategies to treat COVID-19. [Display omitted] •SARS-CoV-2 virus infection or expression of ORF3a blocks formation of autolysosomes•SARS-CoV-2 ORF3a sequestrates the HOPS component VPS39 on late endosomes•SARS-CoV-2 ORF3a impairs the assembly of the STX17-SNAP29-VAMP8 SNARE complex•SARS virus ORF3a fails to interact with VPS39 or affect autophagy activity Miao et al. demonstrate that late endosome-localized ORF3a of the COVID-19 virus SARS-CoV-2 sequestrates the HOPS component VPS39. ORF3a blocks autophagosome/amphisome fusion with lysosomes by preventing the assembly of the STX17-SNAP29-VAMP8 SNARE complex. SARS-CoV-2-infected cells also exhibit a defect in autophagosome maturation and sequestration of VPS39 on late endosomes.
Autophagy acts as a cellular surveillance mechanism to combat invading pathogens. Viruses have evolved various strategies to block autophagy and even subvert it for their replication and release. Here, we demonstrated that ORF3a of the COVID-19 virus SARS-CoV-2 inhibits autophagy activity by blocking fusion of autophagosomes/amphisomes with lysosomes. The late endosome-localized ORF3a directly interacts with and sequestrates the homotypic fusion and protein sorting (HOPS) component VPS39, thereby preventing HOPS complex from interacting with the autophagosomal SNARE protein STX17. This blocks assembly of the STX17-SNAP29-VAMP8 SNARE complex, which mediates autophagosome/amphisome fusion with lysosomes. Expression of ORF3a also damages lysosomes and impairs their function. SARS-CoV-2 virus infection blocks autophagy, resulting in accumulation of autophagosomes/amphisomes, and causes late endosomal sequestration of VPS39. Surprisingly, ORF3a from the SARS virus SARS-CoV fails to interact with HOPS or block autophagy. Our study reveals a mechanism by which SARS-CoV-2 evades lysosomal destruction and provides insights for developing new strategies to treat COVID-19.
Author Shi, Yi
Wang, Peihui
Miao, Guangyan
Bi, Yuhai
Li, Yan
Zhao, Hongyu
Zhang, Hong
Ji, Mingming
Chen, Yong
Author_xml – sequence: 1
  givenname: Guangyan
  surname: Miao
  fullname: Miao, Guangyan
  organization: National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, P.R. China
– sequence: 2
  givenname: Hongyu
  surname: Zhao
  fullname: Zhao, Hongyu
  organization: National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, P.R. China
– sequence: 3
  givenname: Yan
  surname: Li
  fullname: Li, Yan
  organization: CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, P.R. China
– sequence: 4
  givenname: Mingming
  surname: Ji
  fullname: Ji, Mingming
  organization: National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, P.R. China
– sequence: 5
  givenname: Yong
  surname: Chen
  fullname: Chen, Yong
  organization: National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, P.R. China
– sequence: 6
  givenname: Yi
  surname: Shi
  fullname: Shi, Yi
  organization: CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, P.R. China
– sequence: 7
  givenname: Yuhai
  surname: Bi
  fullname: Bi, Yuhai
  organization: CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, P.R. China
– sequence: 8
  givenname: Peihui
  surname: Wang
  fullname: Wang, Peihui
  organization: Advanced Medical Research Institute, Cheeloo College of Medicine, Shandong University, Ji'nan, Shandong 250012, P.R. China
– sequence: 9
  givenname: Hong
  surname: Zhang
  fullname: Zhang, Hong
  email: hongzhang@ibp.ac.cn
  organization: National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, P.R. China
BackLink https://www.ncbi.nlm.nih.gov/pubmed/33422265$$D View this record in MEDLINE/PubMed
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Snippet Autophagy acts as a cellular surveillance mechanism to combat invading pathogens. Viruses have evolved various strategies to block autophagy and even subvert...
SourceID pubmedcentral
proquest
pubmed
crossref
elsevier
SourceType Open Access Repository
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Index Database
Enrichment Source
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StartPage 427
SubjectTerms Autophagosomes - metabolism
Autophagy
Autophagy-Related Proteins - metabolism
COVID-19
COVID-19 - metabolism
COVID-19 - virology
DMV
HEK293 Cells
HeLa Cells
HOPS
Humans
Lysosomes - metabolism
ORF3a
Protein Binding
SARS-CoV-2
SARS-CoV-2 - metabolism
SARS-CoV-2 - pathogenicity
SNARE
SNARE Proteins - metabolism
Vesicular Transport Proteins - metabolism
Viroporin Proteins - genetics
Viroporin Proteins - metabolism
Title ORF3a of the COVID-19 virus SARS-CoV-2 blocks HOPS complex-mediated assembly of the SNARE complex required for autolysosome formation
URI https://dx.doi.org/10.1016/j.devcel.2020.12.010
https://www.ncbi.nlm.nih.gov/pubmed/33422265
https://www.proquest.com/docview/2476853260
https://pubmed.ncbi.nlm.nih.gov/PMC7832235
Volume 56
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