Hemagglutinin of influenza virus partitions into the nonraft domain of model membranes

Nikolaus, Jorg, Scolari, Silvia, Bayraktarov, Elisa, Jungnick, Nadine, Engel, Stephanie, Pia Plazzo, Anna, Stöckl, Martin, Volkmer, Rudolf, Veit, Michael and Herrmann, Andreas (2010) Hemagglutinin of influenza virus partitions into the nonraft domain of model membranes. Biophysical Journal, 99 2: 489-498. doi:10.1016/j.bpj.2010.04.027

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Author Nikolaus, Jorg
Scolari, Silvia
Bayraktarov, Elisa
Jungnick, Nadine
Engel, Stephanie
Pia Plazzo, Anna
Stöckl, Martin
Volkmer, Rudolf
Veit, Michael
Herrmann, Andreas
Title Hemagglutinin of influenza virus partitions into the nonraft domain of model membranes
Journal name Biophysical Journal   Check publisher's open access policy
ISSN 0006-3495
Publication date 2010-07-21
Sub-type Article (original research)
DOI 10.1016/j.bpj.2010.04.027
Open Access Status File (Author Post-print)
Volume 99
Issue 2
Start page 489
End page 498
Total pages 10
Place of publication St. Louis, MO, United States
Publisher Cell Press
Language eng
Abstract The HA of influenza virus is a paradigm for a transmembrane protein thought to be associated with membranerafts, liquid-ordered like nanodomains of the plasma membrane enriched in cholesterol, glycosphingolipids, and saturated phospholipids. Due to their submicron size in cells, rafts can not be visualized directly and raft-association of HA was hitherto analyzed by indirect methods. In this study, we have used GUVs and GPMVs, showing liquid disordered and liquid ordered domains, to directly visualize partition of HA by fluorescence microscopy. We show that HA is exclusively (GUVs) or predominantly (GPMVs) present in the liquid disordered domain, regardless of whether authentic HA or domains containing its raft targeting signals were reconstituted into model membranes. The preferential partition of HA into Id domains and the difference between Io partition in GUV and GPMV are discussed with respect to differences in packaging of lipids in membranes of model systems and living cells suggesting that physical properties of lipid domains in biological membranes are tightly regulated by protein-lipid interactions.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ
Additional Notes http://www.sciencedirect.com/science/article/pii/S0006349510005242#

Document type: Journal Article
Sub-type: Article (original research)
Collection: Global Change Institute Publications
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Citation counts: TR Web of Science Citation Count  Cited 25 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 27 times in Scopus Article | Citations
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Created: Mon, 15 Sep 2014, 15:58:07 EST by Elisa Bayraktarov on behalf of Global Change Institute