Intrinsically-disordered N-termini in human parechovirus 1 capsid proteins bind encapsidated RNA

Show full item record



Permalink

http://hdl.handle.net/10138/237700

Citation

Shakeel , S , Evans , J D , Hazelbaker , M , Kao , C C , Vaughan , R C & Butcher , S J 2018 , ' Intrinsically-disordered N-termini in human parechovirus 1 capsid proteins bind encapsidated RNA ' , Scientific Reports , vol. 8 , no. 1 , 5820 . https://doi.org/10.1038/s41598-018-23552-7

Title: Intrinsically-disordered N-termini in human parechovirus 1 capsid proteins bind encapsidated RNA
Author: Shakeel, Shabih; Evans, James D.; Hazelbaker, Mark; Kao, C. Cheng; Vaughan, Robert C.; Butcher, Sarah J.
Contributor: University of Helsinki, Institute of Biotechnology
University of Helsinki, Institute of Biotechnology
University of Helsinki, Molecular and Integrative Biosciences Research Programme
Date: 2018-04-11
Language: eng
Number of pages: 10
Belongs to series: Scientific Reports
ISSN: 2045-2322
URI: http://hdl.handle.net/10138/237700
Abstract: Human parechoviruses (HPeV) are picornaviruses with a highly-ordered RNA genome contained within icosahedrally-symmetric capsids. Ordered RNA structures have recently been shown to interact with capsid proteins VP1 and VP3 and facilitate virus assembly in HPeV1. Using an assay that combines reversible cross-linking, RNA affinity purification and peptide mass fingerprinting (RCAP), we mapped the RNA-interacting regions of the capsid proteins from the whole HPeV1 virion in solution. The intrinsically-disordered N-termini of capsid proteins VP1 and VP3, and unexpectedly, VP0, were identified to interact with RNA. Comparing these results to those obtained using recombinantly-expressed VP0 and VP1 confirmed the virion binding regions, and revealed unique RNA binding regions in the isolated VP0 not previously observed in the crystal structure of HPeV1. We used RNA fluorescence anisotropy to confirm the RNA-binding competency of each of the capsid proteins’ N-termini. These findings suggests that dynamic interactions between the viral RNA and the capsid proteins modulate virus assembly, and suggest a novel role for VP0.
Subject: BROME MOSAIC-VIRUS
COAT PROTEIN
MASS-SPECTROMETRY
IMMUNE EVASION
VIRAL-RNA
SEQUENCE
IDENTIFICATION
REPLICATION
ANTIBODIES
INITIATION
1182 Biochemistry, cell and molecular biology
Rights:


Files in this item

Total number of downloads: Loading...

Files Size Format View
s41598_018_23552_7.pdf 2.055Mb PDF View/Open

This item appears in the following Collection(s)

Show full item record