Publikationsdatenbank

Site-specific attachment of palmitate or stearate to cytoplasmic versus transmembrane cysteines is a common feature of viral spike proteins (2010)

Art

Zeitschriftenartikel / wissenschaftlicher Beitrag

Autoren

Kordyukova, Larisa V

Serebryakova, Marina V

Baratova, Ludmila A

Veit, Michael

Quelle

Virology

Bandzählung: 398

Heftzählung: 1

Seiten: 49 – 56

ISSN: 0042-6822

Sprache

Englisch

Verweise

DOI: 10.1016/j.virol.2009.11.039

Pubmed: 20006369

Kontakt

Institut für Immunologie

Robert-von-Ostertag-Str. 7-13
14163 Berlin
+49 30 838 51834
immunologie@vetmed.fu-berlin.de

Abstract / Zusammenfassung

Many glycoproteins of enveloped viruses are known to be "palmitoylated" at cysteines located either in the transmembrane region or in the cytoplasmic tail. Although it was recognized early on that "palmitoylation" is not specific for this carbon chain, the exact fatty acid composition of S-acylated proteins has been difficult to determine. Advancements in mass-spectrometry (MS) now allow one to quantify the fatty acids linked to single acylation sites. We report that G of Vesicular Stomatitis virus contains palmitate at a cytoplasmic cysteine, whereas F of Newcastle Disease virus and E1 of Semliki Forest virus (SFV) are stoichiometrically acylated with stearate at a transmembrane cysteine. E2 of SFV contains three molecules of palmitate and one molecule of stearate, the latter probably attached to a transmembrane cysteine. Thus, site-specific attachment of palmitate or stearate, previously described only for HA of influenza virus, is a common feature of viral spike proteins.