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

• Published in: Virology (New York, N.Y.) Vol. 398; no. 1; pp. 49 - 56
• Main Authors: Kordyukova, Larisa V, Serebryakova, Marina V, Baratova, Ludmila A, Veit, Michael
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.03.2010
• Subjects: amino acid sequences; Cell Membrane; Cysteine; Cytoplasm; glycoproteins; host-pathogen relationships; Infectious Disease; Influenza virus; MALDI-TOF MS; molecular sequence data; Newcastle Disease virus; Newcastle disease virus - physiology; Palmitates - chemistry; Palmitates - metabolism; palmitic acid; palmitoylation; pathogenesis; Semliki Forest virus; Semliki forest virus - physiology; Stearates - chemistry; Stearates - metabolism; stearic acid; Vesicular Stomatitis virus; Vesiculovirus; Vesiculovirus - physiology; Viral Envelope Proteins - metabolism; Viral membrane; viral proteins; viral spike protein; MALDI-TOF MS; Semliki Forest virus; Viral membrane; F; G; Newcastle Disease virus; E1; E2; Vesicular Stomatitis virus; palmitoylation
• ISSN: 0042-6822; 1096-0341
• DOI: 10.1016/j.virol.2009.11.039

Abstract 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.