# S-palmitoylation and depalmitoylation at the interface of animal virus-host interactions

## TL;DR

This review explores how reversible S-palmitoylation and depalmitoylation influence interactions between animal viruses and their host cells, focusing on immune evasion and replication.

## Contribution

The paper highlights the underappreciated role of depalmitoylation in virus-host interactions and its impact on viral replication and host defense.

## Key findings

- S-palmitoylation and depalmitoylation regulate viral protein functions during the viral life cycle.
- Viruses exploit these modifications to evade host immune responses.
- Depalmitoylation plays a distinct role in controlling viral replication and host antiviral strategies.

## Abstract

Reversible protein S-palmitoylation, mediated by protein acyl transferases (PATs) and depalmitoylases, is essential for regulating numerous biological processes, including subcellular localization, protein stability, enzymatic activity, and protein-protein interactions. While the study of S-palmitoylation in virology is extensive, less attention has been paid to its reverse process, depalmitoylation, at the virus-host interface. This review summarizes the dynamic regulatory mechanisms of both S-palmitoylation and depalmitoylation. We systematically review the functional consequences of these host enzyme-mediated modifications based on the roles of viral proteins in the viral life cycle. Next, we focus on how viruses exploit these modifications for immune evasion and the corresponding host antiviral strategies. Finally, we analyze the distinct role of depalmitoylation in regulating viral replication and host defense. Overall, this review aims to provide new insights into the regulatory mechanisms of reversible S-palmitoylation at the virus-host interface.