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Differential transport of Influenza A neuraminidase signal anchor peptides to the plasma membrane

Influenza A Neuraminidase is essential for virus release from the cell surface of host cells. Given differential structures of the N-terminal sequences including the transmembrane domains of neuraminidase subtypes, we investigated their contribution to transport and localization of subtypes N1, N2 a...

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Hauptverfasser: Ernst, Andreas M. (VerfasserIn) , Zacherl, Sonja (VerfasserIn) , Herrmann, Alexia (VerfasserIn) , Hacke, Moritz (VerfasserIn) , Nickel, Walter (VerfasserIn) , Wieland, Felix T. (VerfasserIn) , Brügger, Britta (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 21 March 2013
In: FEBS letters
Year: 2013, Jahrgang: 587, Heft: 9, Pages: 1411-1417
ISSN:1873-3468
DOI:10.1016/j.febslet.2013.03.019
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.febslet.2013.03.019
Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S0014579313002305
Volltext
Verfasserangaben:Andreas Max Ernst, Sonja Zacherl, Alexia Herrmann, Moritz Hacke, Walter Nickel, Felix T. Wieland, Britta Brügger
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Zusammenfassung:Influenza A Neuraminidase is essential for virus release from the cell surface of host cells. Given differential structures of the N-terminal sequences including the transmembrane domains of neuraminidase subtypes, we investigated their contribution to transport and localization of subtypes N1, N2 and N8 to the plasma membrane. We generated consensus sequences from all protein entries available for these subtypes. We found that 40N-terminal the forty N-terminal amino acids are sufficient to confer plasma membrane localization of fusion proteins, albeit with different efficiencies. Strikingly, subtle differences in the primary structure of the part of the transmembrane domain that resides in the exoplasmic leaflet of the membrane have a major impact on transport efficiency, providing a potential target for the inhibition of virus release.
Beschreibung:Gesehen am 17.02.2021
Beschreibung:Online Resource
ISSN:1873-3468
DOI:10.1016/j.febslet.2013.03.019

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