Localization of the tryptophan residues of influenza virus matrix protein in reconstructed proteoliposomes: a fluorescent analysis
Dobretsov, G.E.; Zakomyrdin, I.A.; Spirin, M.M.; Booker, D.; Kharitonenkov, I.G.
Voprosy Virusologii 27(4): 432-437
1982
ISSN/ISBN: 0507-4088 PMID: 7135922 Document Number: 197048
Influenza virus matrix protein (M-protein) interaction with model phospholipid membranes, liposomes, was studied. Measuring of the effectiveness of energy transfer from M-protein triptophan residues to a fluorescent zond pyren included into the lipid phase of proteoliposomes was employed to assess the steric organization of the proteoliposome protein-lipid complex. A steric model is proposed in which M-protein molecules are located on the surface of lipid bilayer forming trimers. Analysis of pyren fluorescence proper demonstrated a strong influence of M-protein on the lipid bilayer structure: the viscosity of the lipid phase in the presence of M-protein was increased 2.3-fold.