Intrinsically-disordered N-termini in human parechovirus 1 capsid proteins bind encapsidated RNA
| Autor: | Robert C. Vaughan, James D. Evans, Mark Hazelbaker, C. Cheng Kao, Shabih Shakeel, Sarah J. Butcher |
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| Přispěvatelé: | Institute of Biotechnology, Macromolecular structure and function, Molecular and Integrative Biosciences Research Programme, Doctoral Programme in Microbiology and Biotechnology |
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
Models
Molecular 0301 basic medicine viruses Science Parechovirus IMMUNE EVASION Human parechovirus 1 SEQUENCE Genome Article Virus INITIATION 03 medical and health sciences Peptide mass fingerprinting Brome mosaic virus Virion binding Humans Multidisciplinary IDENTIFICATION 030102 biochemistry & molecular biology biology Chemistry Virus Assembly Virion RNA MASS-SPECTROMETRY biochemical phenomena metabolism and nutrition VIRAL-RNA biology.organism_classification COAT PROTEIN 3. Good health Cell biology BROME MOSAIC-VIRUS Cross-Linking Reagents 030104 developmental biology Capsid REPLICATION ANTIBODIES RNA Viral 1182 Biochemistry cell and molecular biology Medicine Capsid Proteins HT29 Cells |
| Zdroj: | Scientific Reports, Vol 8, Iss 1, Pp 1-10 (2018) Scientific Reports |
| ISSN: | 2045-2322 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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