tetano
Editor, Senior Moderator
Cell Microbiol. 2012 Oct 12. doi: 10.1111/cmi.12045. [Epub ahead of print]
Lipid domain association of influenza virus proteins detected by ynamic fluorescence microscopy techniques.
Veit M, Engel S, Thaa B, Scolari S, Herrmann A.
Source
Free University Berlin, Faculty of Veterinary Medicine, Institute of Immunology, Philippstr. 13, 10115, Berlin, Germany.
Abstract
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).
? 2012 Blackwell Publishing Ltd.
PMID:
23057766
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/23057766
Lipid domain association of influenza virus proteins detected by ynamic fluorescence microscopy techniques.
Veit M, Engel S, Thaa B, Scolari S, Herrmann A.
Source
Free University Berlin, Faculty of Veterinary Medicine, Institute of Immunology, Philippstr. 13, 10115, Berlin, Germany.
Abstract
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).
? 2012 Blackwell Publishing Ltd.
PMID:
23057766
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/23057766