The emerging roles of ZDHHCs-mediated protein palmitoylation in the antiviral innate immune responses

Abstract

Post-translational modifications (PTMs) play a pivotal role in expanding functional protein diversity. During viral infection, pathogen-associated molecular patterns derived from viruses are recognized by pattern recognition receptors present in the membrane surface and the cytoplasm of infected cells, which subsequently induces the antiviral innate immunity to protect the host from the invading viruses. Fatty acylation modification is identified as a post-translation lipid modification process. Mounting evidence is presented that lipid modification functions as a novel regulatory mechanism of antiviral innate immunity. In mammalian cells, DHHC (Asp-His-His-Cys) domain is indispensable for most of the palmitoylation modification, which belongs to fatty acylation. ZDHHC family proteins are composed of 23 members in human cells. In this review, we will summarize the recent findings of the regulatory mechanism of the palmitoylation in the process of host antiviral innate immunity against viruses.

Keywords:

• DHHC (Asp-His-His-Cys) domain
• the palmitoylation
• innate immunity
• viral infection

Acknowledgments

We apologize to all colleagues whose contributions were not discussed and cited owing to space constraints. We are grateful to Sisilia Zheng for the critical review of the manuscript.

Author contributions

YL wrote the manuscript and designed the figures. CZ reviewed and modified the review.

Disclosure statement

No potential conflict of interest was reported by the author(s).

Correction Statement

This article has been corrected with minor changes. These changes do not impact the academic content of the article.

Additional information

Funding

Current work in the Zheng laboratory relevant to this article was supported by grants from the Science and Technology Program of Fujian [2018Y9064].