tetano
Editor, Senior Moderator
Biochem Soc Trans. 2013 Feb 1;41(1):50-5. doi: 10.1042/BST20120210.
Palmitoylation of influenza virus proteins.
Veit M, Serebryakova MV, Kordyukova LV.
Source
*Department of Immunology and Molecular Biology Veterinary Faculty, Free University, Philippstr. 13, 10115 Berlin, Germany.
Abstract
Influenza viruses contain two palmitoylated (S-acylated) proteins: the major spike protein HA (haemagglutinin) and the proton-channel M2. The present review describes the fundamental biochemistry of palmitoylation of HA: the location of palmitoylation sites and the fatty acid species bound to HA. Finally, the functional consequences of palmitoylation of HA and M2 are discussed regarding association with membrane rafts, entry of viruses into target cells by HA-mediated membrane fusion as well as the release of newly assembled virus particles from infected cells.
PMID:
23356257
[PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/23356257
Palmitoylation of influenza virus proteins.
Veit M, Serebryakova MV, Kordyukova LV.
Source
*Department of Immunology and Molecular Biology Veterinary Faculty, Free University, Philippstr. 13, 10115 Berlin, Germany.
Abstract
Influenza viruses contain two palmitoylated (S-acylated) proteins: the major spike protein HA (haemagglutinin) and the proton-channel M2. The present review describes the fundamental biochemistry of palmitoylation of HA: the location of palmitoylation sites and the fatty acid species bound to HA. Finally, the functional consequences of palmitoylation of HA and M2 are discussed regarding association with membrane rafts, entry of viruses into target cells by HA-mediated membrane fusion as well as the release of newly assembled virus particles from infected cells.
PMID:
23356257
[PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/23356257