Please wait a minute...
Protein & Cell

ISSN 1674-800X

ISSN 1674-8018(Online)

CN 11-5886/Q

邮发代号 80-984

2019 Impact Factor: 10.164

Protein & Cell  2024, Vol. 15 Issue (2): 79-82   https://doi.org/10.1093/procel/pwad042
  本期目录
SARS-CoV-2 ORF8 does not function in the nucleus as a histone mimic
Ping Liu1, Junjie Hu1,2, Lei Wang1,2()
1. National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China
2. College of Life Sciences, University of Chinese Academy of Sciences, Beijing 100049, China
 全文: PDF(5777 KB)  
出版日期: 2024-02-28
Corresponding Author(s): Lei Wang   
 引用本文:   
. [J]. Protein & Cell, 2024, 15(2): 79-82.
Ping Liu, Junjie Hu, Lei Wang. SARS-CoV-2 ORF8 does not function in the nucleus as a histone mimic. Protein Cell, 2024, 15(2): 79-82.
 链接本文:  
https://academic.hep.com.cn/pac/CN/10.1093/procel/pwad042
https://academic.hep.com.cn/pac/CN/Y2024/V15/I2/79
1 B Alberts, J Alexander, L Julian et al. Chapter 12-Intracellular Compartments and Protein Sorting. Molecular biology of the cell (6th ed.). New York: Garland Science, 2015, 649–50.
2 K Barroso, E. Chevet Chapter 15-Epigenetic regulation of endoplasmic reticulum stress. Chromatin Signaling and Diseases. Boston: Academic Press, 2016, 271–85.
https://doi.org/10.1016/B978-0-12-802389-1.00015-0
3 TG Flower, CZ Buffalo, RM Hooy et al. Structure of SARS-CoV-2 ORF8, a rapidly evolving immune evasion protein. Proc Natl Acad Sci U S A 2021;118:e2021785118.
https://doi.org/10.1073/pnas.2021785118
4 TS Fung, DX. Liu Coronavirus infection, ER stress, apoptosis and innate immunity. Front Microbiol 2014;5:296.
https://doi.org/10.3389/fmicb.2014.00296
5 YM Go, DP. Jones Redox compartmentalization in eukaryotic cells. Biochim Biophys Acta 2008;1780:1273–90.
https://doi.org/10.1016/j.bbagen.2008.01.011
6 Q Guo, S Sidoli, BA Garcia et al. Assessment of quantification precision of histone post-translational modifications by using an ion trap and down To 50 000 cells as starting material. J Proteome Res 2018;17:234–42.
https://doi.org/10.1021/acs.jproteome.7b00544
7 DP Ha, R Van Krieken, AJ Carlos et al. The stress-inducible molecular chaperone GRP78 as potential therapeutic target for coronavirus infection. J Infect 2020;81:452–82.
https://doi.org/10.1016/j.jinf.2020.06.017
8 J Kee, S Thudium, DM Renner et al. SARS-CoV-2 disrupts host epigenetic regulation via histone mimicry. Nature 2022;610:381–88.
https://doi.org/10.1038/s41586-022-05282-z
9 E Kohli, S Causse, V Baverel et al. Endoplasmic reticulum chaperones in viral infection: therapeutic perspectives. Microbiol Mol Biol Rev 2021;85:e0003521.
https://doi.org/10.1128/MMBR.00035-21
10 P Liu, X Wang, Y Sun et al. SARS-CoV-2 ORF8 reshapes the ER through forming mixed disulfides with ER oxidoreductases. Redox Biol 2022;54:102388.
https://doi.org/10.1016/j.redox.2022.102388
11 Z Ozturkler, R. Kalkan A new perspective of COVID-19 infection: an epigenetics point of view. Glob Med Genet 2021;9:4–6.
https://doi.org/10.1055/s-0041-1736565
12 WJ Shin, DP Ha, K Machida et al. The stress-inducible ER chaperone GRP78/BiP is upregulated during SARS-CoV-2 infection and acts as a pro-viral protein. Nat Commun 2022;13:6551.
https://doi.org/10.1038/s41467-022-34065-3
13 S Vinjamuri, L Li, M. Bouvier SARS-CoV-2 ORF8: one protein, seemingly one structure, and many functions. Front Immunol 2022;13:1035559.
https://doi.org/10.3389/fimmu.2022.1035559
14 L Wang, CC. Wang Oxidative protein folding fidelity and redoxtasis in the endoplasmic reticulum. Trends Biochem Sci 2023;48:40–52.
https://doi.org/10.1016/j.tibs.2022.06.011
15 M Xue, L. Feng The role of unfolded protein response in coronavirus infection and its implications for drug design. Front Microbiol 2021;12:808593.
https://doi.org/10.3389/fmicb.2021.808593
Viewed
Full text


Abstract

Cited

  Shared   
  Discussed