1887

Abstract

The matrix (M) protein isolated from influenza A/WSN/33 virus, when reconstituted with ribonucleo-protein (RNP) cores of vesicular stomatitis virus (VSV), resulted in inhibition of VSV transcription . The presence of endogenous wild-type (wt) or mutant (O23) VSV matrix (M) protein on RNP cores did not prevent down-regulation of VSV transcription by reconstituted influenza virus M protein. In fact, endogenous VSV wt M protein augmented transcription inhibition by M protein reconstituted with RNP/M protein cores, whereas mutant O23 M protein endogenous to RNP cores had no effect on down-regulation of VSV transcription by M protein. These data suggest that VSV M protein and influenza virus M protein recognize two different sites on RNP cores responsible for down-regulation of VSV transcription. Monoclonal antibodies (MAbs) directed to epitope 2 of M protein had been previously shown to reverse transcription inhibition by M protein on influenza virus RNP cores, but the same epitope 2-specific MAb had little effect on transcription inhibition by M protein reconstituted with VSV RNP cores. VSV M protein bears a striking resemblance biologically and genetically to the M protein, including, as shown here, their capacity to bind viral RNA. However, the VSV wt M protein exhibited no capacity to down-regulate transcription by influenza virus RNP cores. The significance of these studies is the identification on VSV RNP templates of at least two separate sites for recognition of protein factors that repress VSV transcription.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-73-3-743
1992-03-01
2019-10-17
Loading full text...

Full text loading...

http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-73-3-743
Loading

Most Cited This Month

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error