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Published in: Virology Journal 1/2017

Open Access 01-12-2017 | Short Report

The nonstructural proteins of Pneumoviruses are remarkably distinct in substrate diversity and specificity

Authors: Michael Ribaudo, Sailen Barik

Published in: Virology Journal | Issue 1/2017

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Abstract

Background

Interferon (IFN) inhibits viruses by inducing several hundred cellular genes, aptly named ‘interferon (IFN)-stimulated genes’ (ISGs). The only two RNA viruses of the Pneumovirus genus of the Paramyxoviridae family, namely Respiratory Syncytial Virus (RSV) and Pneumonia Virus of Mice (PVM), each encode two nonstructural (NS) proteins that share no sequence similarity but yet suppress IFN. Since suppression of IFN underlies the ability of these viruses to replicate in the host cells, the mechanism of such suppression has become an important area of research. This Short Report is an important extension of our previous efforts in defining this mechanism.

Results

We show that, like their PVM counterparts, the RSV NS proteins also target multiple members of the ISG family. While significantly extending the substrate repertoire of the RSV NS proteins, these results, unexpectedly, also reveal that the target preferences of the NS proteins of the two viruses are entirely different. This is surprising since the two Pneumoviruses are phylogenetically close with similar genome organization and gene function, and the NS proteins of both also serve as suppressors of host IFN response.

Conclusion

The finding that the NS proteins of the two highly similar viruses suppress entirely different members of the ISG family raises intriguing questions of pneumoviral NS evolution and mechanism of action.
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Metadata
Title
The nonstructural proteins of Pneumoviruses are remarkably distinct in substrate diversity and specificity
Authors
Michael Ribaudo
Sailen Barik
Publication date
01-12-2017
Publisher
BioMed Central
Published in
Virology Journal / Issue 1/2017
Electronic ISSN: 1743-422X
DOI
https://doi.org/10.1186/s12985-017-0881-7

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