SARS-CoV-2 ORF8 does not function in the nucleus as a histone mimic

Ping Liu, Junjie Hu, Lei Wang

PDF(5777 KB)
PDF(5777 KB)
Protein Cell ›› 2024, Vol. 15 ›› Issue (2) : 79-82. DOI: 10.1093/procel/pwad042
OPINION

SARS-CoV-2 ORF8 does not function in the nucleus as a histone mimic

Author information +
History +

Cite this article

Download citation ▾
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 https://doi.org/10.1093/procel/pwad042

References

[1]
Alberts B, Alexander J, Julian L et al. Chapter 12-Intracellular Compartments and Protein Sorting. Molecular biology of the cell (6th ed.). New York: Garland Science, 2015, 649–50.
[2]
Barroso K, Chevet E. Chapter 15-Epigenetic regulation of endoplasmic reticulum stress. Chromatin Signaling and Diseases. Boston: Academic Press, 2016, 271–85.
CrossRef Google scholar
[3]
Flower TG, Buffalo CZ, Hooy RM et al. Structure of SARS-CoV-2 ORF8, a rapidly evolving immune evasion protein. Proc Natl Acad Sci U S A 2021;118:e2021785118.
CrossRef Google scholar
[4]
Fung TS, Liu DX. Coronavirus infection, ER stress, apoptosis and innate immunity. Front Microbiol 2014;5:296.
CrossRef Google scholar
[5]
Go YM, Jones DP. Redox compartmentalization in eukaryotic cells. Biochim Biophys Acta 2008;1780:1273–90.
CrossRef Google scholar
[6]
Guo Q, Sidoli S, Garcia BA 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.
CrossRef Google scholar
[7]
Ha DP, Van Krieken R, Carlos AJ et al. The stress-inducible molecular chaperone GRP78 as potential therapeutic target for coronavirus infection. J Infect 2020;81:452–82.
CrossRef Google scholar
[8]
Kee J, Thudium S, Renner DM et al. SARS-CoV-2 disrupts host epigenetic regulation via histone mimicry. Nature 2022;610:381–88.
CrossRef Google scholar
[9]
Kohli E, Causse S, Baverel V et al. Endoplasmic reticulum chaperones in viral infection: therapeutic perspectives. Microbiol Mol Biol Rev 2021;85:e0003521.
CrossRef Google scholar
[10]
Liu P, Wang X, Sun Y et al. SARS-CoV-2 ORF8 reshapes the ER through forming mixed disulfides with ER oxidoreductases. Redox Biol 2022;54:102388.
CrossRef Google scholar
[11]
Ozturkler Z, Kalkan R. A new perspective of COVID-19 infection: an epigenetics point of view. Glob Med Genet 2021;9:4–6.
CrossRef Google scholar
[12]
Shin WJ, Ha DP, Machida K 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.
CrossRef Google scholar
[13]
Vinjamuri S, Li L, Bouvier M. SARS-CoV-2 ORF8: one protein, seemingly one structure, and many functions. Front Immunol 2022;13:1035559.
CrossRef Google scholar
[14]
Wang L, Wang CC. Oxidative protein folding fidelity and redoxtasis in the endoplasmic reticulum. Trends Biochem Sci 2023;48:40–52.
CrossRef Google scholar
[15]
Xue M, Feng L. The role of unfolded protein response in coronavirus infection and its implications for drug design. Front Microbiol 2021;12:808593.
CrossRef Google scholar

RIGHTS & PERMISSIONS

2023 The Author(s) 2023. Published by Oxford University Press on behalf of Higher Education Press.
AI Summary AI Mindmap
PDF(5777 KB)

Accesses

Citations

Detail

Sections
Recommended

/