Membrane penetration of Sendai virus glycoproteins during the early stages of fusion with liposomes as determined by hydrophobic photoaffinity labeling.
AUTOR(ES)
Novick, S L
RESUMO
The hydrophobic photoaffinity label 3-(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine was used to label Sendai virus proteins during fusion with cardiolipin and phosphatidylserine liposomes. Preferential labeling of the viral fusion protein during the initial stages of fusion demonstrated that this protein interacts with the hydrophobic core of the target membrane as an initiating event of virus-liposome fusion. Labeling showed time, temperature, and pH dependence consistent with earlier fluorescent measurements of fusion kinetics. The present method provides conclusive evidence supporting the hypothesis that hydrophobic interaction of the fusion protein with the target bilayer is an initial event in the fusion mechanism of viral membranes.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=282205Documentos Relacionados
- Identity of hepatic membrane transport systems for bile salts, phalloidin, and antamanide by photoaffinity labeling.
- Juvenile hormone receptors in insect larval epidermis: identification by photoaffinity labeling.
- Guanosine 3',5'-cyclic nucleotide binding proteins of bovine retina identified by photoaffinity labeling.
- Subcellular distribution of gentamicin in proximal tubular cells, determined by immunogold labeling.
- Interaction of a nuclear location signal with isolated nuclear envelopes and identification of signal-binding proteins by photoaffinity labeling.