Lipid domain association of influenza virus proteins detected by dynamic fluorescence microscopy techniques.
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.
Institute of Immunology, Free University Berlin, Philippstr. 13, 10115 Berlin, Germany. mveit@zedat.fu-berlin.de
Michael
M
Veit
Stephanie
S
Engel
Bastian
B
Thaa
Silvia
S
Scolari
Andreas
A
Herrmann
D000818:Animals; D016466:CHO Cells; D006224:Cricetinae; D036681:Fluorescence Recovery After Photobleaching; D031541:Fluorescence Resonance Energy Transfer; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D021962:Membrane Microdomains / Q000737:chemistry* / Q000378:metabolism / Q000821:virology; D008856:Microscopy, Fluorescence; D009975:Orthomyxoviridae / Q000737:chemistry* / Q000502:physiology; D014162:Transfection; D014763:Viral Matrix Proteins / Q000737:chemistry / Q000378:metabolism*; D019065:Virus Assembly; D014779:Virus Replication; D000086082:Viroporin Proteins
D019267:Hemagglutinin Glycoproteins, Influenza Virus; D014763:Viral Matrix Proteins; C488937:M2 protein, Influenza A virus; D000086082:Viroporin Proteins