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Lipid domain association of influenza virus proteins detected by ynamic fluorescence microscopy techniques.
MedLine Citation:
PMID:  23057766     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
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. For a more comprehensive treatment of raft-association of influenza virus proteins and budding of viral particles the reader is referred to several recent reviews (Chen et al., 2008a, Nayak et al., 2009, Nayak et al., 2004, Rossman et al., 2011, Veit et al., 2011).
Authors:
Michael Veit; Stephanie Engel; Bastian Thaa; Silvia Scolari; Andreas Herrmann
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-10-12
Journal Detail:
Title:  Cellular microbiology     Volume:  -     ISSN:  1462-5822     ISO Abbreviation:  Cell. Microbiol.     Publication Date:  2012 Oct 
Date Detail:
Created Date:  2012-10-12     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100883691     Medline TA:  Cell Microbiol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
© 2012 Blackwell Publishing Ltd.
Affiliation:
Free University Berlin, Faculty of Veterinary Medicine, Institute of Immunology, Philippstr. 13, 10115, Berlin, Germany.
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