这是用户在 2025-8-7 17:34 为 https://pubmed.ncbi.nlm.nih.gov/35155279/ 保存的双语快照页面，由 沉浸式翻译 提供双语支持。了解如何保存？
Skip to main page content
U.S. flag

An official website of the United States government

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2022 Jan 27:12:821596.
doi: 10.3389/fcimb.2022.821596. eCollection 2022.

Protein Palmitoylation Modification During Viral Infection and Detection Methods of Palmitoylated Proteins

Xiaoling Li  1 , Lingyi Shen  1 , Zhao Xu  1 , Wei Liu  1 , Aihua Li  2 , Jun Xu  1
Affiliations
Review

Protein Palmitoylation Modification During Viral Infection and Detection Methods of Palmitoylated Proteins

Xiaoling Li et al. Front Cell Infect Microbiol. .

Abstract

Protein palmitoylation-a lipid modification in which one or more cysteine thiols on a substrate protein are modified to form a thioester with a palmitoyl group-is a significant post-translational biological process. This process regulates the trafficking, subcellular localization, and stability of different proteins in cells. Since palmitoylation participates in various biological processes, it is related to the occurrence and development of multiple diseases. It has been well evidenced that the proteins whose functions are palmitoylation-dependent or directly involved in key proteins' palmitoylation/depalmitoylation cycle may be a potential source of novel therapeutic drugs for the related diseases. Many researchers have reported palmitoylation of proteins, which are crucial for host-virus interactions during viral infection. Quite a few explorations have focused on figuring out whether targeting the acylation of viral or host proteins might be a strategy to combat viral diseases. All these remarkable achievements in protein palmitoylation have been made to technological advances. This paper gives an overview of protein palmitoylation modification during viral infection and the methods for palmitoylated protein detection. Future challenges and potential developments are proposed.

Keywords: S-palmitoylation; detection methods; post-translational modification; viral infection; virus-host interaction.

PubMed Disclaimer

Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

Figure 1
Figure 1
Protein palmitoylation/depalmitoylation cycle.
Figure 2
Figure 2
Schematic diagram of Acyl-PEGyl exchange gel-shift (APEGS) assay.
Figure 3
Figure 3
The diagram of the detailed procedures of APEGS for cell samples.

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Abdulrahman D. A., Meng X., Veit M. (2021). S-Acylation of Proteins of Coronavirus and Influenza Virus: Conservation of Acylation Sites in Animal Viruses and DHHC Acyltransferases in Their Animal Reservoirs. Pathogens 10 (6), 669. doi: 10.3390/pathogens10060669 - DOI - PMC - PubMed
    1. Akerstrom S., Gunalan V., Keng C. T., Tan Y. J., Mirazimi A. (2009). Dual Effect of Nitric Oxide on SARS-CoV Replication: Viral RNA Production and Palmitoylation of the S Protein Are Affected. Virology 395 (1), 1–9. doi: 10.1016/j.virol.2009.09.007 - DOI - PMC - PubMed
    1. Azizi S. A., Lan T., Delalande C., Kathayat R. S., Banales Mejia F., Qin A., et al. . (2021). Development of an Acrylamide-Based Inhibitor of Protein S-Acylation. ACS Chem. Biol. 16 (8), 1546–1556. doi: 10.1021/acschembio.1c00405 - DOI - PMC - PubMed
    1. Bakhache W., Neyret A., Bernard E., Merits A., Briant L. (2020). Palmitoylated Cysteines in Chikungunya Virus Nsp1 Are Critical for Targeting to Cholesterol-Rich Plasma Membrane Microdomains With Functional Consequences for Viral Genome Replication. J. Virol. 94 (10), e02183–19. doi: 10.1128/JVI.02183-19 - DOI - PMC - PubMed
    1. Batistic O., Sorek N., Schultke S., Yalovsky S., Kudla J. (2008). Fatty Acyl Modification Determines the Localization and Plasma Membrane Targeting of CBL/CIPK Ca2+ Signaling Complexes in Arabidopsis. Plant Cell 20 (5), 1346–1362. doi: 10.1105/tpc.108.058123 - DOI - PMC - PubMed

Publication types