Norovirus VPg Binds RNA through a Conserved N-Terminal K/R Basic Patch
In: Viruses, Jg. 13 (2021-06-01), Heft 7, S. 1282
Online
academicJournal
Zugriff:
The viral protein genome-linked (VPg) of noroviruses is a multi-functional protein that participates in essential roles during the viral replication cycle. Predictive analyses indicate that murine norovirus (MNV) VPg contains a disordered N-terminal region with RNA binding potential. VPg proteins were expressed with an N-terminal spidroin fusion protein in insect cells and the interaction with RNA investigated by electrophoretic mobility shift assays (EMSA) against a series of RNA probes (pentaprobes) representing all possible five nucleotide combinations. MNV VPg and human norovirus (HuNV) VPg proteins were directly bound to RNA in a non-specific manner. To identify amino acids involved in binding to RNA, all basic (K/R) residues in the first 12 amino acids of MNV VPg were mutated to alanine. Removal of the K/R amino acids eliminated RNA binding and is consistent with a K/R basic patch RNA binding motif within the disordered N-terminal region of norovirus VPgs. Finally, we show that mutation of the K/R basic patch required for RNA binding eliminates the ability of MNV VPg to induce a G0/G1 cell cycle arrest.
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Norovirus VPg Binds RNA through a Conserved N-Terminal K/R Basic Patch
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Autor/in / Beteiligte Person: | McSweeney, Alice M. ; Young, Vivienne L. ; Ward, Vernon K. |
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Zeitschrift: | Viruses, Jg. 13 (2021-06-01), Heft 7, S. 1282 |
Veröffentlichung: | MDPI AG, 2021 |
Medientyp: | academicJournal |
ISSN: | 1999-4915 (print) |
DOI: | 10.3390/v13071282 |
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