Enhancement of membrane-fusing activity of sendai virus by exposure of the virus to basic pH is correlated with a conformational change in the fusion protein.
The effect of pH on the membrane-fusion activity of Sendai virus was examined (pH 5.0-9.5) by using, as assays of activity, hemolysis of chicken erythrocytes and the fusion of baby hamster kidney (BHK-21) cells. Exposure of virus to basic pH increased fusion activity; the optimum pH was found to be approximately equal to 9.0. All assays were carried out at pH 7.0, and the virus retained enhanced fusion activity after it was exposed to basic pH and returned to neutral pH. The enhanced fusion activity was correlated with an irreversible conformational change in the fusion protein (F protein) of the virus, as demonstrated by a change in the circular dichroism spectrum of the protein.
D000818:Animals; D002460:Cell Line; D002642:Chick Embryo; D002942:Circular Dichroism; D006224:Cricetinae; D006461:Hemolysis; D006863:Hydrogen-Ion Concentration; D007668:Kidney; D007700:Kinetics; D010222:Parainfluenza Virus 1, Human / Q000502:physiology*; D011487:Protein Conformation; D011991:Receptors, Virus / Q000378:metabolism*; D014760:Viral Fusion Proteins; D014764:Viral Proteins / Q000378:metabolism*
D011991:Receptors, Virus; D014760:Viral Fusion Proteins; D014764:Viral Proteins