Publikationsdatenbank

Acylation and cholesterol binding are not required for targeting of influenza A virus M2 protein to the hemagglutinin-defined budozone (2014)

Art

Zeitschriftenartikel / wissenschaftlicher Beitrag

Autoren

Thaa, Bastian (WE 5)

Siche, Stefanie (WE 5)

Herrmann, Andreas

Veit, Michael (WE 5)

Quelle

FEBS letters; 588(6) — S. 1031–1036

ISSN: 0014-5793

Verweise

DOI: 10.1016/j.febslet.2014.02.014

Pubmed: 24561202

Kontakt

Institut für Virologie

Robert-von-Ostertag-Str. 7-13
Gebäude 35
14163 Berlin
+49 30 838 51833
viro@zedat.fu-berlin.de

Abstract / Zusammenfassung

Influenza virus assembles in the budozone, a cholesterol-/sphingolipid-enriched ("raft") domain at the apical plasma membrane, organized by hemagglutinin (HA). The viral protein M2 localizes to the budozone edge for virus particle scission. This was proposed to depend on acylation and cholesterol binding. We show that M2-GFP without these motifs is still transported apically in polarized cells. Employing FRET, we determined that clustering between HA and M2 is reduced upon disruption of HA's raft-association features (acylation, transmembranous VIL motif), but remains unchanged with M2 lacking acylation and/or cholesterol-binding sites. The motifs are thus irrelevant for M2 targeting in cells.