Publikationsdatenbank

Differential S-acylation of Enveloped Viruses (2019)

Art

Zeitschriftenartikel / wissenschaftlicher Beitrag

Autoren

Kordyukova, Larisa V.

Serebryakova, Marina V.

Khrustalev, Vladislav V.

Veit, Michael (WE 5)

Quelle

Protein and peptide letters

Bandzählung: 26

Heftzählung: 8

Seiten: 588 – 600

ISSN: 1875-5305

Sprache

Englisch

Verweise

URL (Volltext): http://www.eurekaselect.com/172377/article

DOI: 10.2174/0929866526666190603082521

Pubmed: 31161979

Kontakt

Institut für Virologie

Robert-von-Ostertag-Str. 7-13
14163 Berlin
+49 30 838 51833
virologie@vetmed.fu-berlin.de

Abstract / Zusammenfassung

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 palmitoyl-proteomes 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.