Protein Acetylation Going Viral: Implications in Antiviral Immunity and Viral Infection

Abstract

During viral infection, both host and viral proteins undergo post-translational modifications (PTMs), including phosphorylation, ubiquitination, methylation, and acetylation, which play critical roles in viral replication, pathogenesis, and host antiviral responses. Protein acetylation is one of the most important PTMs and is catalyzed by a series of acetyltransferases that divert acetyl groups from acetylated molecules to specific amino acid residues of substrates, affecting chromatin structure, transcription, and signal transduction, thereby participating in the cell cycle as well as in metabolic and other cellular processes. Acetylation of host and viral proteins has emerging roles in the processes of virus adsorption, invasion, synthesis, assembly, and release as well as in host antiviral responses. Methods to study protein acetylation have been gradually optimized in recent decades, providing new opportunities to investigate acetylation during viral infection. This review summarizes the classification of protein acetylation and the standard methods used to map this modification, with an emphasis on viral and host protein acetylation during viral infection.

Role of protein Post-translational modifications in enterovirus infection

“…Protein acetylation affects numerous biological events, including gene replication, transcription, repair, and signal transduction pathways; thereby regulating diverse cellular processes ( Arnesen, 2011 ; Verdin and Ott, 2015 ). Host and viral proteins undergo acetylation which can play pivotal roles in different phases of viral infection, including viral entry, genome replication, assembly and release of progeny viral particles, and host antiviral responses ( Murray et al, 2018 ; Xue et al, 2022 ). With the rapid development and optimization of proteomics and mass spectrometry technologies, a new era of protein acetylation research during viral infection has recently emerged.…”

“…The progression of PTMs is dynamic, reversible, and catalyzed by specific enzymes; therefore, many compounds targeting these enzymes can effectively inhibit or promote PTM ( Lopez et al, 2016 ; Sun et al, 2020 ; Zhu et al, 2022c ). Different PTMs on different host and viral proteins can exert various effects on viral growth by targeting viral entry, replication, assembly, egress, and antiviral immune response ( Kumar et al, 2020 ; Song et al, 2021 ; Cheng et al, 2022 ; Xue et al, 2022 ). Here, we review some essential PTMs, including ubiquitination, phosphorylation, acetylation, SUMOylation, tyrosine sulfation, neddylation, and ISGylation, associated with host-pathogen interactions to better understand the role and mechanism of PTMs during enterovirus infection.…”

Influenza A Virus and Acetylation: The Picture Is Becoming Clearer

“…However, acetylation is now known to be ubiquitous, occurs on both histone and non-histone proteins, and is known to play a critical role in diverse cellular processes [ 38 , 44 , 45 ]. As a modification, acetylation influences protein stability and folding, protein–protein interactions, and protein trafficking and subcellular localization; hence, it is critical in cellular metabolism and cellular response to stress [ 36 , 38 , 39 , 46 ]. Any imbalance in acetylation via aberrant activity or expression of the HATs, NATs, or HDACs in humans contributes to various cancers and cardiovascular, inflammatory and infectious diseases, and developmental, neurodegenerative, and genetic disorders [ 47 , 48 ].…”

Histone acetylation gene‐based biomarkers as novel markers of the immune microenvironment in glioblastoma

“…9,10 Protein acetylation of both histones and non-histones plays an important role in a variety of cellular activities, in both normal and abnormal cells. [11][12][13] With the introduction of the concept of the tumour microenvironment, 14,15 there is increasing evidence that changes in the tumour microenvironment, that is, the microenvironment in which tumour cells survive and interact with their surrounding stroma and immune cells, play an important and irreplaceable role in tumourigenesis, progression and metastasis. [16][17][18] Histone acetylation can not only participate in and influence the function of immune cells infiltrating the microenvironment, but also participate in the remodelling of the tumour microenvironment by regulating the secretory function of immune cells, stromal cells and tumour cells.…”

“…This modification is a reversible post‐translational modification and acetylation allows proteins to have multiple structures, which in turn produce functional diversity, finer regulation and more specific action 9,10 . Protein acetylation of both histones and non‐histones plays an important role in a variety of cellular activities, in both normal and abnormal cells 11–13 . With the introduction of the concept of the tumour microenvironment, 14,15 there is increasing evidence that changes in the tumour microenvironment, that is, the microenvironment in which tumour cells survive and interact with their surrounding stroma and immune cells, play an important and irreplaceable role in tumourigenesis, progression and metastasis 16–18 .…”