Please use this identifier to cite or link to this item:
https://doi.org/10.1371/journal.ppat.1002030
DC Field | Value | |
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dc.title | The hexamer structure of the Rift Valley fever virus nucleoprotein suggests a mechanism for its assembly into ribonucleoprotein complexes | |
dc.contributor.author | Ferron F. | |
dc.contributor.author | Li Z. | |
dc.contributor.author | Danek E.I. | |
dc.contributor.author | Luo D. | |
dc.contributor.author | Wong Y. | |
dc.contributor.author | Coutard B. | |
dc.contributor.author | Lantez V. | |
dc.contributor.author | Charrel R. | |
dc.contributor.author | Canard B. | |
dc.contributor.author | Walz T. | |
dc.contributor.author | Lescar J. | |
dc.date.accessioned | 2020-03-13T05:26:47Z | |
dc.date.available | 2020-03-13T05:26:47Z | |
dc.date.issued | 2011 | |
dc.identifier.citation | Ferron F., Li Z., Danek E.I., Luo D., Wong Y., Coutard B., Lantez V., Charrel R., Canard B., Walz T., Lescar J. (2011). The hexamer structure of the Rift Valley fever virus nucleoprotein suggests a mechanism for its assembly into ribonucleoprotein complexes. PLoS Pathogens 7 (5) : e1002030. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.ppat.1002030 | |
dc.identifier.issn | 15537366 | |
dc.identifier.uri | https://scholarbank.nus.edu.sg/handle/10635/165414 | |
dc.description.abstract | Rift Valley fever virus (RVFV), a Phlebovirus with a genome consisting of three single-stranded RNA segments, is spread by infected mosquitoes and causes large viral outbreaks in Africa. RVFV encodes a nucleoprotein (N) that encapsidates the viral RNA. The N protein is the major component of the ribonucleoprotein complex and is also required for genomic RNA replication and transcription by the viral polymerase. Here we present the 1.6 Å crystal structure of the RVFV N protein in hexameric form. The ring-shaped hexamers form a functional RNA binding site, as assessed by mutagenesis experiments. Electron microscopy (EM) demonstrates that N in complex with RNA also forms rings in solution, and a single-particle EM reconstruction of a hexameric N-RNA complex is consistent with the crystallographic N hexamers. The ring-like organization of the hexamers in the crystal is stabilized by circular interactions of the N terminus of RVFV N, which forms an extended arm that binds to a hydrophobic pocket in the core domain of an adjacent subunit. The conformation of the N-terminal arm differs from that seen in a previous crystal structure of RVFV, in which it was bound to the hydrophobic pocket in its own core domain. The switch from an intra- to an inter-molecular interaction mode of the N-terminal arm may be a general principle that underlies multimerization and RNA encapsidation by N proteins from Bunyaviridae. Furthermore, slight structural adjustments of the N-terminal arm would allow RVFV N to form smaller or larger ring-shaped oligomers and potentially even a multimer with a super-helical subunit arrangement. Thus, the interaction mode between subunits seen in the crystal structure would allow the formation of filamentous ribonucleocapsids in vivo. Both the RNA binding cleft and the multimerization site of the N protein are promising targets for the development of antiviral drugs. © 2011 Ferron et al. | |
dc.publisher | Public Library of Science | |
dc.source | Unpaywall 20200320 | |
dc.subject | guanine nucleotide binding protein | |
dc.subject | nucleoprotein | |
dc.subject | oligomer | |
dc.subject | ribonucleoprotein | |
dc.subject | RNA | |
dc.subject | complementary DNA | |
dc.subject | hybrid protein | |
dc.subject | nucleocapsid protein | |
dc.subject | ribonucleoprotein | |
dc.subject | virus RNA | |
dc.subject | amino terminal sequence | |
dc.subject | article | |
dc.subject | binding site | |
dc.subject | Bunyavirus | |
dc.subject | crystal structure | |
dc.subject | crystallization | |
dc.subject | crystallography | |
dc.subject | electron microscopy | |
dc.subject | hydrophobicity | |
dc.subject | in vivo study | |
dc.subject | molecular interaction | |
dc.subject | mutagenesis | |
dc.subject | nonhuman | |
dc.subject | nucleotide sequence | |
dc.subject | protein assembly | |
dc.subject | protein conformation | |
dc.subject | protein multimerization | |
dc.subject | Rift Valley fever bunyavirus | |
dc.subject | RNA binding | |
dc.subject | amino acid sequence | |
dc.subject | animal | |
dc.subject | chemical structure | |
dc.subject | chemistry | |
dc.subject | genetics | |
dc.subject | human | |
dc.subject | isolation and purification | |
dc.subject | metabolism | |
dc.subject | methodology | |
dc.subject | physiology | |
dc.subject | protein domain | |
dc.subject | protein multimerization | |
dc.subject | sequence alignment | |
dc.subject | site directed mutagenesis | |
dc.subject | surface plasmon resonance | |
dc.subject | ultrastructure | |
dc.subject | virus assembly | |
dc.subject | X ray crystallography | |
dc.subject | Bunyaviridae | |
dc.subject | Phlebovirus | |
dc.subject | Rift Valley fever virus | |
dc.subject | Amino Acid Sequence | |
dc.subject | Animals | |
dc.subject | Crystallography, X-Ray | |
dc.subject | DNA, Complementary | |
dc.subject | Humans | |
dc.subject | Microscopy, Electron | |
dc.subject | Models, Molecular | |
dc.subject | Mutagenesis, Site-Directed | |
dc.subject | Nucleocapsid Proteins | |
dc.subject | Protein Interaction Domains and Motifs | |
dc.subject | Protein Multimerization | |
dc.subject | Recombinant Fusion Proteins | |
dc.subject | Ribonucleoproteins | |
dc.subject | Rift Valley fever virus | |
dc.subject | RNA, Viral | |
dc.subject | Sequence Alignment | |
dc.subject | Surface Plasmon Resonance | |
dc.subject | Virus Assembly | |
dc.type | Article | |
dc.contributor.department | DUKE-NUS MEDICAL SCHOOL | |
dc.description.doi | 10.1371/journal.ppat.1002030 | |
dc.description.sourcetitle | PLoS Pathogens | |
dc.description.volume | 7 | |
dc.description.issue | 5 | |
dc.description.page | e1002030 | |
dc.published.state | Published | |
Appears in Collections: | Staff Publications Elements |
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