AI Article Synopsis
- Influenza virus assembles in a specialized membrane area called the budozone, primarily organized by the protein hemagglutinin (HA).
- The protein M2 is located at the edge of this region for the release of new virus particles, a process thought to depend on specific molecular interactions.
- Research using FRET technology reveals that while disruptions to HA's membrane association decrease its clustering with M2, M2's targeting to the budozone does not rely on its own acylation or cholesterol-binding sites.
Article 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.
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| http://dx.doi.org/10.1016/j.febslet.2014.02.014 | DOI Listing |
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