Open AccessLipid domain association of influenza virus proteins detected by dynamic fluorescence microscopy techniques
Author(s) -
Veit Michael,
Engel Stephanie,
Thaa Bastian,
Scolari Silvia,
Herrmann Andreas
Publication year - 2013
Publication title -
cellular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.542
H-Index - 138
eISSN - 1462-5822
pISSN - 1462-5814
DOI - 10.1111/cmi.12045
Subject(s) - fluorescence microscope , lipid raft , virus , biology , förster resonance energy transfer , sted microscopy , transfection , microscopy , domain (mathematical analysis) , influenza a virus , microbiology and biotechnology , raft , lipid bilayer , virology , fluorescence , computational biology , biophysics , membrane , biochemistry , chemistry , gene , signal transduction , mathematics , mathematical analysis , optics , polymer , quantum mechanics , physics , organic chemistry , copolymer , laser , stimulated emission
Summary Influenza virus is thought to assemble in raft domains of the plasma membrane, but many of the conclusions were based on (controversial) Triton extraction experiments. Here we review how sophisticated methods of fluorescence microscopy, such as FPALM , FRET and FRAP , contributed to our understanding of lipid domain association of the viral proteins HA and M2 . The results are summarized in light of the current model for virus assembly and lipid domain organization. Finally, it is described how the signals that govern domain association in transfected cells affect replication of influenza virus.