tetano
Editor, Senior Moderator
FEBS Lett. 2014 Feb 20. pii: S0014-5793(14)00133-1. doi: 10.1016/j.febslet.2014.02.014. [Epub ahead of print]
Acylation and cholesterol binding are not required for targeting of influenza A virus M2 protein to the hemagglutinin-defined budozone.
Thaa B1, Siche S1, Herrmann A2, Veit M3.
Author information
Abstract
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.
Copyright ? 2014. Published by Elsevier B.V.
KEYWORDS:
Apical transport, Hemagglutinin, Influenza virus, M2, Palmitoylation, Raft localization
PMID:
24561202
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24561202
Acylation and cholesterol binding are not required for targeting of influenza A virus M2 protein to the hemagglutinin-defined budozone.
Thaa B1, Siche S1, Herrmann A2, Veit M3.
Author information
Abstract
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.
Copyright ? 2014. Published by Elsevier B.V.
KEYWORDS:
Apical transport, Hemagglutinin, Influenza virus, M2, Palmitoylation, Raft localization
PMID:
24561202
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24561202