Genome encapsidation by orthobunyavirus nucleoproteins

Zheng, Wei; Tao, Yizhi Jane

doi:10.1073/pnas.1306838110

Cited by 8 publications

(7 citation statements)

References 21 publications

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“…By negative-stain electron microscopy, we observed filamentous RNP scaffolds with a diameter of 10–12.5 nm that may have an underlying helical sub-pattern (Figure 1C ). The morphology of these RNPs was reminiscent of that of orthobunyavirus RNPs ( 18–21 , 40 ), but differed from those reported for RVFV that showed a more extended conformation ( 23–24 ).…”

Section: Resultsmentioning

confidence: 70%

Structural insights into RNA encapsidation and helical assembly of the Toscana virus nucleoprotein

Olal

Dick

Woods

et al. 2014

Nucleic Acids Research

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Toscana virus is an emerging bunyavirus in Mediterranean Europe where it accounts for 80% of pediatric meningitis cases during the summer. The negative-strand ribonucleic acid (RNA) genome of the virus is wrapped around the virally encoded nucleoprotein N to form the ribonucleoprotein complex (RNP). We determined crystal structures of hexameric N alone (apo) and in complex with a nonameric single-stranded RNA. RNA is sequestered in a sequence-independent fashion in a deep groove inside the hexamer. At the junction between two adjacent copies of Ns, RNA binding induced an inter-subunit rotation, which opened the RNA-binding tunnel and created a new assembly interface at the outside of the hexamer. Based on these findings, we suggest a structural model for how binding of RNA to N promotes the formation of helical RNPs, which are a characteristic hallmark of many negative-strand RNA viruses.

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Section: Resultsmentioning

confidence: 70%

Structural insights into RNA encapsidation and helical assembly of the Toscana virus nucleoprotein

Olal

Dick

Woods

et al. 2014

Nucleic Acids Research

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“…Actually, N proteins of CCHFV, which belongs to the genus Nairovirus, showed a helical organization even in the crystal, implying that this organization reflects their vRNP structure in living cells (20). The N proteins of the other three genera of the family Bunyaviridae have been reported to form smaller ring structures (3-to 6-mers) than those of nsNSVs in crystals (14)(15)(16)(17)(22)(23)(24)(25)(26)(27)(28)(29). In most previous reports, it was suggested that the N protein rings of the genera Phlebovirus, Hantavirus, and Orthobunyavirus were rearranged to form coiled vRNPs when they enwrap a long genomic RNA on the basis of their two-dimensional (2D) EM images (26,27,43).…”

Section: Discussionmentioning

confidence: 99%

“…For the genus Nairovirus, some oligomerization states (monomer and superhelical organizations) of N proteins have been reported (18)(19)(20)(21). N proteins of several viruses of the genus Orthobunyavirus were determined as tetramer ring structures in crystals (22)(23)(24)(25)(26)(27)(28). Finally, the N protein of the genus Hantavirus has been reported to be a hexamer ring in crystals (29).…”

mentioning

confidence: 99%

Asymmetric Trimeric Ring Structure of the Nucleocapsid Protein of Tospovirus

Komoda

Narita

Yamashita

et al. 2017

J Virol

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(TSWV), belonging to the genus of the family, causes significant economic damage to several vegetables and ornamental plants worldwide. Similar to those of all other negative-strand RNA viruses, the nucleocapsid (N) protein plays very important roles in its viral life cycle. N proteins protect genomic RNAs by encapsidation and form a viral ribonucleoprotein complex (vRNP) with some RNA-dependent RNA polymerases. Here we show the crystal structure of the N protein from TSWV. Protomers of TSWV N proteins consist of three parts: the N arm, C arm, and core domain. Unlike N proteins of other negative-strand RNA viruses, the TSWV N protein forms an asymmetric trimeric ring. To form the trimeric ring, the N and C arms of the N protein interact with the core domains of two adjacent N proteins. By solving the crystal structures of the TSWV N protein with nucleic acids, we showed that an inner cleft of the asymmetric trimeric ring is an RNA-binding site. These characteristics are similar to those of N proteins of other viruses of the family Based on these observations, we discuss possibilities of a TSWV encapsidation model. Tospoviruses cause significant crop losses throughout the world. Particularly, TSWV has an extremely wide host range (>1,000 plant species, including dicots and monocots), and worldwide losses are estimated to be in excess of $1 billion annually. Despite such importance, no proteins of tospoviruses have been elucidated so far. Among TSWV-encoded proteins, the N protein is required for assembling the viral genomic RNA into the viral ribonucleoprotein (vRNP), which is involved in various steps of the life cycle of these viruses, such as RNA replication, virus particle formation, and cell-to-cell movement. This study revealed the structure of the N protein, with or without nucleic acids, of TSWV as the first virus of the genus , so it completed our view of the N proteins of the family.

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“…All members of the Bunyaviridae encode less well‐conserved accessory proteins as well, and these are found on the M or S segments (NSm/NSs). The N protein encapsidates each of the RNA segments to form a ribonucleoprotein complex (RNP), which associates with the RdRp [44]. The viral glycoproteins Gn and Gc are translated from the M segment as a polyprotein precursor, which is translocated into the endoplasmic reticulum (ER) where it is co‐ and post‐translationally processed into the individual glycoproteins.…”

Section: Biotechnological Production Of Arboviral Evlps and Their Vmentioning

confidence: 99%

Enveloped virus‐like particles as vaccines against pathogenic arboviruses

Pijlman

2015

Biotechnology Journal

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Arthropod-borne arboviruses form a continuous threat to human and animal health, but few arboviral vaccines are currently available. Advances in expression technology for complex, enveloped virus-like particles (eVLPs) create new opportunities to develop potent vaccines against pathogenic arboviruses. In this short review, I highlight the successes and challenges in eVLP production for members of the three major arbovirus families: Flaviviridae (e.g., dengue, West Nile, Japanese encephalitis); Bunyaviridae (e.g., Rift Valley fever); and Togaviridae (e.g., chikungunya). The results from pre-clinical testing will be discussed as well as specific constraints to the large-scale manufacture and purification of eVLPs, which are complex assemblies of membranes and viral glycoproteins. Insect cells emerge as ideal substrates for correct arboviral glycoprotein folding and posttranslational modification to yield high quality eVLPs. Furthermore, baculovirus expression in insect cell culture is scalable and has a proven safety record in industrial human and veterinary vaccine manufacturing. In conclusion, eVLPs produced in insect cells using modern biotechnology have a realistic potential to be used in novel vaccines against arboviral diseases.

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Genome encapsidation by orthobunyavirus nucleoproteins

Cited by 8 publications

References 21 publications

Structural insights into RNA encapsidation and helical assembly of the Toscana virus nucleoprotein

Structural insights into RNA encapsidation and helical assembly of the Toscana virus nucleoprotein

Asymmetric Trimeric Ring Structure of the Nucleocapsid Protein of Tospovirus

Enveloped virus‐like particles as vaccines against pathogenic arboviruses

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