The Glycoprotein Cytoplasmic Tail of Uukuniemi Virus (
            <i>Bunyaviridae</i>
            ) Interacts with Ribonucleoproteins and Is Critical for Genome Packaging

Överby, Anna K.; Pettersson, Ralf F.; Neve, Etienne P.A.

doi:10.1128/jvi.02655-06

Cited by 80 publications

(84 citation statements)

References 48 publications

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“…Based on this observation, it was suggested that the cytoplasmic tails of the viral glycoproteins might bind the viral ribonucleoprotein (6). Indeed, recent results have shown that the G1 tail binds the viral ribonucleoprotein in phlebovirus (7) and is required for packaging the genome in orthobunyavirus (8). These data suggest that the G1 tail plays a critical role in viral assembly.…”

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confidence: 77%

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The Hantavirus Glycoprotein G1 Tail Contains Dual CCHC-type Classical Zinc Fingers

Estrada

Boudreaux

Zhong

et al. 2009

Journal of Biological Chemistry

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Hantaviruses are distributed worldwide and can cause a hemorrhagic fever or a cardiopulmonary syndrome in humans. Mature virions consist of RNA genome, nucleocapsid protein, RNA polymerase, and two transmembrane glycoproteins, G1 and G2. The ectodomain of G1 is surface-exposed; however, it has a 142-residue C-terminal cytoplasmic tail that plays important roles in viral assembly and host-pathogen interaction. Here we show by NMR, circular dichroism spectroscopy, and mutagenesis that a highly conserved cysteine/histidine-rich region in the G1 tail of hantaviruses forms two CCHC-type classical zinc fingers. Unlike classical zinc fingers, however, the two G1 zinc fingers are intimately joined together, forming a compact domain with a unique fold. We discuss the implication of the hantaviral G1 zinc fingers in viral assembly and host-pathogen interaction.

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confidence: 77%

“…The G1 tail of Bunyaviriade viruses is important in viral assembly (7,8) and host-pathogen interaction (9 -13). Our results showed that a conserved cysteine/histidinerich region in the hantavirus G1 tail (Fig.…”

Section: Discussionmentioning

confidence: 99%

The Hantavirus Glycoprotein G1 Tail Contains Dual CCHC-type Classical Zinc Fingers

Estrada

Boudreaux

Zhong

et al. 2009

Journal of Biological Chemistry

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“…Like the polymerase, which catalyses RNA replication and transcription by cap-snatching (6), NP is multifunctional. In coating exclusively genomic or antigenomic viral RNA (but not viral mRNA or cellular RNA), it protects the viral genome from degradation, avoids formation of dsRNA between viral RNAs of opposite polarity, compacts the RNA into RNPs, and by interacting with the glycoprotein tails inside the virion membrane, actively promotes packaging into progeny virions (7,8). Dynamic interactions of NP with the polymerase are also critical, allowing the polymerase controlled access to the RNA within template RNPs on the one hand and nucleating assembly of progeny RNPs only when the polymerase is functioning as a replicase.…”

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confidence: 99%

Structural basis for encapsidation of genomic RNA by La Crosse Orthobunyavirus nucleoprotein

Reguera

Malet

Weber

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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The nucleoprotein (NP) of segmented negative-strand RNA viruses such as Orthomyxo-, Arena-, and Bunyaviruses coats the genomic viral RNA and together with the polymerase forms ribonucleoprotein particles (RNPs), which are both the template for replication and transcription and are packaged into new virions. Here we describe the crystal structure of La Crosse Orthobunyavirus NP both RNA free and a tetrameric form with single-stranded RNA bound. La Crosse Orthobunyavirus NP is a largely helical protein with a fold distinct from other bunyavirus genera NPs. It binds 11 RNA nucleotides in the positively charged groove between its two lobes, and hinged N-and C-terminal arms mediate oligomerization, allowing variable protein-protein interface geometry. Oligomerization and RNA binding are mediated by residues conserved in the Orthobunyavirus genus. In the twofold symmetric tetramer, 44 nucleotides bind in a closed ring with sharp bends at the NP-NP interfaces. The RNA is largely inaccessible within a continuous internal groove. Electron microscopy of RNPs released from virions shows them capable of forming a hierarchy of more or less compact irregular helical structures. We discuss how the planar, tetrameric NP-RNA structure might relate to a polar filament that upon supercoiling could be packaged into virions. This work gives insight into the RNA encapsidation and protection function of bunyavirus NP, but also highlights the need for dynamic rearrangements of the RNP to give the polymerase access to the template RNA.protein-RNA interactions | structural biology T he largest family of segmented negative-strand RNA viruses (sNSVs), Bunyaviridae, comprises more than 350 species belonging to five genera: Orthobunyavirus, Phlebovirus, Nairovirus, Hantavirus, and Tospovirus. Bunyaviruses generally infect mammals, except Tospoviruses that infect plants, and use arthropods as vectors for their spread, although Hantaviruses are rodent borne (1, 2). Several species can cause severe zoonotic diseases in humans such as La Crosse Orthobunyavirus (LACV, childhood encephalitis), Rift Valley Fever Phlebovirus (RVFV), and Crimean Congo Haemorrhagic Fever Nairovirus (CCHFV). As vector-borne diseases, their geographical occurrence is closely linked to the environment, and climate change or other ecological factors may lead to altered distribution or emergence of new viruses (3-5).Bunyaviruses have a trisegmented negative-strand RNA genome. The L segment encodes for the RNA-dependent RNA polymerase or L protein, the M segment for glycoproteins and a nonstructural protein, and the S segment encodes the nucleoprotein (NP) and another nonstructural protein. The genome is always coated by multiple copies of NP forming ribonucleoprotein particles (RNPs), which also contain the viral polymerase. RNPs are the only form under which the genome is efficiently replicated and transcribed, and NP and L are necessary and sufficient to perform these functions. Like the polymerase, which catalyses RNA replication and transcription by cap-snatching (6), ...

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“…RVFV N is thought to interact with the viral RdRp because N is essential to replication and transcription (4). N also plays a role in virus assembly through interactions with the viral envelope glycoproteins (G N and G C ) (5).…”

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Structure of the Rift Valley fever virus nucleocapsid protein reveals another architecture for RNA encapsidation

Raymond¹,

Piper²,

Gerrard

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

117

146

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Rift Valley fever virus (RVFV) is a negative-sense RNA virus (genus Phlebovirus, family Bunyaviridae) that infects livestock and humans and is endemic to sub-Saharan Africa. Like all negative-sense viruses, the segmented RNA genome of RVFV is encapsidated by a nucleocapsid protein (N). The 1.93-Å crystal structure of RVFV N and electron micrographs of ribonucleoprotein (RNP) reveal an encapsidated genome of substantially different organization than in other negative-sense RNA virus families. The RNP polymer, viewed in electron micrographs of both virus RNP and RNP reconstituted from purified N with a defined RNA, has an extended structure without helical symmetry. N-RNA species of ∼100-kDa apparent molecular weight and heterogeneous composition were obtained by exhaustive ribonuclease treatment of virus RNP, by recombinant expression of N, and by reconstitution from purified N and an RNA oligomer. RNA-free N, obtained by denaturation and refolding, has a novel all-helical fold that is compact and well ordered at both the N and C termini. Unlike N of other negative-sense RNA viruses, RVFV N has no positively charged surface cleft for RNA binding and no protruding termini or loops to stabilize a defined N-RNA oligomer or RNP helix. A potential protein interaction site was identified in a conserved hydrophobic pocket. The nonhelical appearance of phlebovirus RNP, the heterogeneous ∼100-kDa N-RNA multimer, and the N fold differ substantially from the RNP and N of other negative-sense RNA virus families and provide valuable insights into the structure of the encapsidated phlebovirus genome.ribonucleoprotein | viral protein | segmented genome | negative-sense RNA virus

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The Glycoprotein Cytoplasmic Tail of Uukuniemi Virus ( Bunyaviridae ) Interacts with Ribonucleoproteins and Is Critical for Genome Packaging

Cited by 80 publications

References 48 publications

The Hantavirus Glycoprotein G1 Tail Contains Dual CCHC-type Classical Zinc Fingers

The Hantavirus Glycoprotein G1 Tail Contains Dual CCHC-type Classical Zinc Fingers

Structural basis for encapsidation of genomic RNA by La Crosse Orthobunyavirus nucleoprotein

Structure of the Rift Valley fever virus nucleocapsid protein reveals another architecture for RNA encapsidation

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