Interaction of wild-type and mutant M protein vesicular stomatitis virus with nucleocapsids in vitro.
We have characterized the interactions between mutant or wild-type M protein and nucleocapsids of vesicular stomatitis virus (VSV) by assaying for inhibition of in vitro transcriptase activity. The interactions are primarily electrostatic in nature: high concentrations of NaCl or poly(L-glutamic acid) reverse the inhibition. These interactions are much weaker in each of the four M protein mutants (complementation group III) tested than in wild-type VSV. Temperature-sensitive revertants were selected from each of the M protein mutants studied. The salt-dependent inhibitory profiles of all the revertants resemble that of wild-type VSV, suggesting that M-nucleocapsid interactions are integrally related to the temperature-sensitive phenotype of group III mutants. These results are discussed in relation to the accompanying paper [Reidler, J.A., Keller, P.M., Elson, E.L., & Lenard, J. (1981) Biochemistry (preceding paper in this issue)] which shows that interaction between M protein and infected cell membranes is increased in all group III mutants studied.
D000818:Animals; D002213:Capsid / Q000378:metabolism*; D002460:Cell Line; D002472:Cell Transformation, Viral; D006224:Cricetinae; D007668:Kidney; D007700:Kinetics; D009154:Mutation; D017830:Octoxynol; D009994:Osmolar Concentration; D011092:Polyethylene Glycols / Q000494:pharmacology; D012965:Sodium Chloride / Q000494:pharmacology; D013696:Temperature; D014158:Transcription, Genetic; D014721:Vesicular stomatitis Indiana virus / Q000378:metabolism*; D014763:Viral Matrix Proteins; D014764:Viral Proteins / Q000096:biosynthesis* / Q000378:metabolism*
D014763:Viral Matrix Proteins; D014764:Viral Proteins; D011092:Polyethylene Glycols; D012965:Sodium Chloride; D017830:Octoxynol