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NSP9 of SARS-CoV-2 attenuates nuclear transport by hampering nucleoporin 62 dynamics and functions in host cells.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2022 Jan 01; Vol. 586, pp. 137-142. Date of Electronic Publication: 2021 Nov 20. - Publication Year :
- 2022
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Abstract
- Nuclear pore complexes (NPC) regulate molecular traffics on nuclear envelope, which plays crucial roles during cell fate specification and diseases. The viral accessory protein NSP9 of SARS-CoV-2 is reported to interact with nucleoporin 62 (NUP62), a structural component of the NPC, but its biological impact on the host cell remain obscure. Here, we established new cell line models with ectopic NSP9 expression and determined the subcellular destination and biological functions of NSP9. Confocal imaging identified NSP9 to be largely localized in close proximity to the endoplasmic reticulum. In agreement with the subcellular distribution of NSP9, association of NSP9 with NUP62 was observed in cytoplasm. Furthermore, the overexpression of NSP9 correlated with a reduction of NUP62 expression on the nuclear envelope, suggesting that attenuating NUP62 expression might have contributed to defective NPC formation. Importantly, the loss of NUP62 impaired translocation of p65, a subunit of NF-κB, upon TNF-α stimulation. Concordantly, NSP9 over-expression blocked p65 nuclear transport. Taken together, these data shed light on the molecular mechanisms underlying the modulation of host cells during SARS-CoV-2 infection.<br />Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.<br /> (Copyright © 2021 The Author(s). Published by Elsevier Inc. All rights reserved.)
- Subjects :
- Active Transport, Cell Nucleus
Endoplasmic Reticulum metabolism
Endoplasmic Reticulum virology
Gene Knockdown Techniques
HeLa Cells
Humans
Membrane Glycoproteins antagonists & inhibitors
Membrane Glycoproteins genetics
Models, Biological
Nuclear Envelope metabolism
Nuclear Envelope virology
Nuclear Pore Complex Proteins antagonists & inhibitors
Nuclear Pore Complex Proteins genetics
RNA-Binding Proteins genetics
Recombinant Fusion Proteins genetics
Recombinant Fusion Proteins metabolism
Transcription Factor RelA metabolism
Viral Nonstructural Proteins genetics
COVID-19 metabolism
COVID-19 virology
Host Microbial Interactions physiology
Membrane Glycoproteins metabolism
Nuclear Pore Complex Proteins metabolism
RNA-Binding Proteins metabolism
SARS-CoV-2 metabolism
Viral Nonstructural Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1090-2104
- Volume :
- 586
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 34844119
- Full Text :
- https://doi.org/10.1016/j.bbrc.2021.11.046