Protein Palmitoylation and Its Role in Bacterial and Viral Infections.

Justyna Sobocińska,Paula Roszczenko-Jasińska,Katarzyna Kwiatkowska,Anna Ciesielska

doi:10.3389/fimmu.2017.02003

Justyna Sobocińska, Paula Roszczenko-Jasińska + Show 2 more

Open Access

https://doi.org/10.3389/fimmu.2017.02003

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Abstract

S-palmitoylation is a reversible, enzymatic posttranslational modification of proteins in which palmitoyl chain is attached to a cysteine residue via a thioester linkage. S-palmitoylation determines the functioning of proteins by affecting their association with membranes, compartmentalization in membrane domains, trafficking, and stability. In this review, we focus on S-palmitoylation of proteins, which are crucial for the interactions of pathogenic bacteria and viruses with the host. We discuss the role of palmitoylated proteins in the invasion of host cells by bacteria and viruses, and those involved in the host responses to the infection. We highlight recent data on protein S-palmitoylation in pathogens and their hosts obtained owing to the development of methods based on click chemistry and acyl-biotin exchange allowing proteomic analysis of protein lipidation. The role of the palmitoyl moiety present in bacterial lipopolysaccharide and lipoproteins, contributing to infectivity and affecting recognition of bacteria by innate immune receptors, is also discussed.

Highlights

Palmitic acid (C16:0) is a long-chain saturated fatty acid, and a component of various lipids playing important roles in cell membrane organization, signal transduction, and energy storage
We focus on S-palmitoylation of proteins crucial for the interactions of pathogenic bacteria and viruses with the host
Protein S-palmitoylation affects their localization, trafficking, and stability. It has long been known as an important factor controlling signal transduction by the B cell receptor (BCR) and T cell receptor (TCR) receptors involved in acquired immune responses

Summary

Introduction

Palmitic acid (C16:0) is a long-chain saturated fatty acid, and a component of various lipids playing important roles in cell membrane organization, signal transduction, and energy storage. Given the large variety of chemical reporters preferentially mimicking distinct fatty acids, recent years have witnessed a plethora of chemistry-based proteomic studies on palmitoylated and myristoylated proteins and proteins bearing the GPI anchor, including those of pathogens and immune cells [10, 14, 85, 86, 114].

Results

Conclusion