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Protein & Peptide Letters

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Review Article

Differential S-acylation of Enveloped Viruses

Author(s): Larisa V. Kordyukova*, Marina V. Serebryakova, Vladislav V. Khrustalev and Michael Veit

Volume 26, Issue 8, 2019

Page: [588 - 600] Pages: 13

DOI: 10.2174/0929866526666190603082521

Abstract

Post-translational modifications often regulate protein functioning. Covalent attachment of long chain fatty acids to cysteine residues via a thioester linkage (known as protein palmitoylation or S-acylation) affects protein trafficking, protein-protein and protein-membrane interactions. This post-translational modification is coupled to membrane fusion or virus assembly and may affect viral replication in vitro and thus also virus pathogenesis in vivo. In this review we outline modern methods to study S-acylation of viral proteins and to characterize palmitoylproteomes of virus infected cells. The palmitoylation site predictor CSS-palm is critically tested against the Class I enveloped virus proteins. We further focus on identifying the S-acylation sites directly within acyl-peptides and the specific fatty acid (e.g, palmitate, stearate) bound to them using MALDI-TOF MS-based approaches. The fatty acid heterogeneity/ selectivity issue attracts now more attention since the recently published 3D-structures of two DHHC-acyl-transferases gave a hint how this might be achieved.

Keywords: Enveloped viruses, influenza virus, S-acylation, palmitate, stearate, MALDI-TOF MS, DHHC-acyl-transferases.

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