Membrane penetration of Sendai virus glycoproteins during the early stages of fusion with liposomes as determined by hydrophobic photoaffinity labeling
The hydrophobic photoaffinity label 3-(trifluoromethyl)-3-(m-(/sup 125/I)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.
- Research Organization:
- California Institute of Technology, Pasadena (USA)
- OSTI ID:
- 6868760
- Journal Information:
- Proc. Natl. Acad. Sci. U.S.A.; (United States), Vol. 85:20
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
GLUCOPROTEINS
LABELLING
AFFINITY
CELL MEMBRANES
IODINE 125
LIPOSOMES
MEMBRANE PROTEINS
SCINTILLATION COUNTING
TEMPERATURE DEPENDENCE
TIME DEPENDENCE
TRACER TECHNIQUES
VIRUSES
BETA DECAY RADIOISOTOPES
CARBOHYDRATES
CELL CONSTITUENTS
COUNTING TECHNIQUES
DAYS LIVING RADIOISOTOPES
ELECTRON CAPTURE RADIOISOTOPES
GLYCOPROTEINS
INTERMEDIATE MASS NUCLEI
IODINE ISOTOPES
ISOTOPE APPLICATIONS
ISOTOPES
MEMBRANES
MICROORGANISMS
NUCLEI
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
ORGANOIDS
PARASITES
PROTEINS
RADIOISOTOPES
SACCHARIDES
550201* - Biochemistry- Tracer Techniques