Publication Database

Palmitoylation of the Alphacoronavirus TGEV spike protein S is essential for incorporation into virus-like particles but dispensable for S-M interaction (2014)

Art

Zeitschriftenartikel / wissenschaftlicher Beitrag

Autoren

Gelhaus, Sandra

Thaa, Bastian

Eschke, Kathrin (WE 5)

Veit, Michael (WE 5)

Schwegmann-Weßels, Christel

Quelle

Virology

Bandzählung: 464-465

Seiten: 397 – 405

ISSN: 0042-6822

Sprache

Englisch

Verweise

DOI: 10.1016/j.virol.2014.07.035

Pubmed: 25113909

Kontakt

Institut für Virologie

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

Abstract / Zusammenfassung

The spike protein S of coronaviruses contains a highly conserved cytoplasmic cysteine-rich motif adjacent to the transmembrane region. This motif is palmitoylated in the Betacoronaviruses MHV and SARS-CoV. Here, we demonstrate by metabolic labeling with [(3)H]-palmitic acid that the S protein of transmissible gastroenteritis coronavirus (TGEV), an Alphacoronavirus, is palmitoylated as well. This is relevant for TGEV replication as virus growth was compromised by the general palmitoylation inhibitor 2-bromopalmitate. Mutation of individual cysteine clusters in the cysteine-rich motif of S revealed that all cysteines must be replaced to abolish acylation and incorporation of S into virus-like particles (VLP). Conversely, the interaction of S with the M protein, essential for VLP incorporation of S, was not impaired by lack of palmitoylation. Thus, palmitoylation of the S protein of Alphacoronaviruses is dispensable for S-M interaction, but required for the generation of progeny virions.