Evidence for an interaction between the membrane protein of a paramyxovirus and actin.
Evidence for an interaction of the membrane (M) protein of Newcastle disease and Sendai viruses with cellular actin was obtained by three different techniques. M protein linked to Sepharose 4B was found to bind actin, but not myoglobin or bovine serum albumin, and to selectively remove actin from a mixture of these three proteins. Sedimentation of a mixture of M protein and F-actin through a sucrose gradient resulted in sedimentation of M protein with actin. Control proteins, bovine serum albumin and cytochrome c, did not sediment with actin. In circular dichroism studies, M protein added to actin in a 1:1 complex resulted in a significant increase in negative ellipticity at 220 nm, which corresponds to an increase in alpha-helix and a decrease in beta-structure and random coil. This is indicative of an interaction between M protein and actin. It is possible that the frequent identification of cellular actin in a number of enveloped viruses may be attributed to the interaction of actin and M protein or its equivalent.
D000199:Actins; D002499:Centrifugation, Density Gradient; D055598:Chemical Phenomena; D002621:Chemistry; D002846:Chromatography, Affinity; D002942:Circular Dichroism; D009522:Newcastle disease virus / Q000032:analysis*; D010222:Parainfluenza Virus 1, Human / Q000032:analysis*; D014763:Viral Matrix Proteins; D014764:Viral Proteins
D000199:Actins; D014763:Viral Matrix Proteins; D014764:Viral Proteins