Activation of the virion-associated RNA polymerase of vesicular stomatitis virus by melittin

Melittin, a major protein of bee venom, interacts with lipoprotein envelope of vesicular stomatitis virus. This interaction results in expression of the virion-associated transcriptase. The RNA synthetic properties of melittin-treated virions are similar to those previously observed with detergent-d...

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Published inBiochemical and biophysical research communications Vol. 105; no. 4; pp. 1265 - 1271
Main Authors Roy, Jayasri, Chanda, Pranab K., Thornton, George B., Luk, Daniel, Banerjee, Amiya K.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 29.04.1982
Subjects
Animals
Bee Venoms - pharmacology
Cell Line
Cricetinae
DNA-Directed RNA Polymerases - metabolism
Enzyme Activation
Kidney
Kinetics
Melitten - pharmacology
Microscopy, Electron
Transcription, Genetic - drug effects
Vesicular stomatitis Indiana virus - drug effects
Vesicular stomatitis Indiana virus - enzymology
Vesicular stomatitis Indiana virus - ultrastructure
vesicular stomatitis virus
Virion - enzymology
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Summary:Melittin, a major protein of bee venom, interacts with lipoprotein envelope of vesicular stomatitis virus. This interaction results in expression of the virion-associated transcriptase. The RNA synthetic properties of melittin-treated virions are similar to those previously observed with detergent-disrupted virions. In contrast to detergent-disruption melittin treatment does not affect the infectivity of the virions. Electron microscopic studies confirm that the melittin-disrupted virions maintain the native structure of the virus.
Bibliography:8225314
L73
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ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(82)90923-8