Mimicking influenza virus fusion using supported lipid bilayers

Influenza virus infection is a serious public health problem in the world, and understanding the molecular mechanisms involved in viral replication is crucial. In this paper, we used a minimalist approach based on a lipid bilayer supported on mica, which we imaged by atomic force microscopy (AFM) in...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1999. - 30(2014), 38 vom: 30. Sept., Seite 11394-400
1. Verfasser: Godefroy, Cédric (VerfasserIn)
Weitere Verfasser: Dahmane, Selma, Dosset, Patrice, Adam, Olivier, Nicolai, Marie-Claire, Ronzon, Frédéric, Milhiet, Pierre-Emmanuel
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2014
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Aluminum Silicates Lipid Bilayers Ribonucleoproteins mica V8A1AW0880
Beschreibung
Zusammenfassung:Influenza virus infection is a serious public health problem in the world, and understanding the molecular mechanisms involved in viral replication is crucial. In this paper, we used a minimalist approach based on a lipid bilayer supported on mica, which we imaged by atomic force microscopy (AFM) in a physiological buffer, to analyze the different steps of influenza fusion, from the interaction of intact viruses with the supported bilayer to their complete fusion. Our results show that sialic acid recognition and priming upon acidification are sufficient for a complete fusion with the host cell membrane. After fusion, a flat and continuous membrane was observed. Because of the fragility of the viral membrane that was removed by the tip, most probably due to the disorganization of the matrix layer at acidic pH, fine structural details of ribonucleoproteins (RNP) were obtained. In addition, AFM topography of intact virus in interaction with the supported lipid bilayer confirms that hemeagglutinin and neuraminidase can form isolated clusters within the viral membrane
Beschreibung:Date Completed 02.07.2015
Date Revised 19.11.2015
published: Print-Electronic
Citation Status MEDLINE
ISSN:1520-5827
DOI:10.1021/la502591a