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  Line-tension controlled mechanism for influenza fusion.

Risselada, H. J., Marelli, G., Fuhrmans, M., Smirnova, Y. G., Grubmüller, H., Marrink, S. J., et al. (2012). Line-tension controlled mechanism for influenza fusion. PLoS One, 7(6): e38302. doi:10.1371/journal.pone.0038302.

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 Urheber:
Risselada, H. J.1, Autor           
Marelli, G., Autor
Fuhrmans, M., Autor
Smirnova, Y. G., Autor
Grubmüller, H.1, Autor           
Marrink, S. J., Autor
Müller , M., Autor
Affiliations:
1Department of Theoretical and Computational Biophysics, MPI for biophysical chemistry, Max Planck Society, ou_578631              

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 Zusammenfassung: Our molecular simulations reveal that wild-type influenza fusion peptides are able to stabilize a highly fusogenic pre-fusion structure, i.e. a peptide bundle formed by four or more trans-membrane arranged fusion peptides. We rationalize that the lipid rim around such bundle has a non-vanishing rim energy (line-tension), which is essential to (i) stabilize the initial contact point between the fusing bilayers, i.e. the stalk, and (ii) drive its subsequent evolution. Such line-tension controlled fusion event does not proceed along the hypothesized standard stalk-hemifusion pathway. In modeled influenza fusion, single point mutations in the influenza fusion peptide either completely inhibit fusion (mutants G1V and W14A) or, intriguingly, specifically arrest fusion at a hemifusion state (mutant G1S). Our simulations demonstrate that, within a linetension controlled fusion mechanism, these known point mutations either completely inhibit fusion by impairing the peptide’s ability to stabilize the required peptide bundle (G1V and W14A) or stabilize a persistent bundle that leads to a kinetically trapped hemifusion state (G1S). In addition, our results further suggest that the recently discovered leaky fusion mutant G13A, which is known to facilitate a pronounced leakage of the target membrane prior to lipid mixing, reduces the membrane integrity by forming a ‘super’ bundle. Our simulations offer a new interpretation for a number of experimentally observed features of the fusion reaction mediated by the prototypical fusion protein, influenza hemagglutinin, and might bring new insights into mechanisms of other viral fusion reactions.

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Sprache(n): eng - English
 Datum: 2012-06-28
 Publikationsstatus: Online veröffentlicht
 Seiten: 14
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1371/journal.pone.0038302
 Art des Abschluß: -

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Titel: PLoS One
Genre der Quelle: Zeitschrift
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Seiten: - Band / Heft: 7 (6) Artikelnummer: e38302 Start- / Endseite: - Identifikator: -