Structural Studies of Hantaan Virus

Battisti, Anthony J.; Chu, Yong-Kyu; Chipman, Paul R.; Kaufmann, Bärbel; Jonsson, Colleen B.; Rossmann, Michael G.

doi:10.1128/jvi.01847-10

Cited by 85 publications

(115 citation statements)

References 27 publications

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“…Further, isolated surface projections could be distinguished (Fig. 2G, arrows), resembling a Y-shape similar to the described molecular structure of Hantaan virus and Tula virus spikes that are composed of a tetrameric, globular head domain connected to the membrane by a thinner, central stalk region (4,5).…”

supporting

confidence: 66%

“…They expose glycoprotein spikes locally ordered into tetramers and also contain naked membrane patches on their surfaces (4,5). The viral envelope membrane is acquired from infected cells during virus budding and encloses the three single-stranded RNA (ssRNA) segments that encode four structural proteins: the Gn and Gc glycoproteins, nucleocapsid protein (N), and RNA-dependent RNA polymerase.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Hantavirus Gn and Gc Glycoproteins Self-Assemble into Virus-Like Particles

Acuña

Cifuentes-Muñoz

Márquez

et al. 2014

J Virol

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f How hantaviruses assemble and exit infected cells remains largely unknown. Here, we show that the expression of Andes (ANDV) and Puumala (PUUV) hantavirus Gn and Gc envelope glycoproteins lead to their self-assembly into virus-like particles (VLPs) which were released to cell supernatants. The viral nucleoprotein was not required for particle formation. Further, a Gc endodomain deletion mutant did not abrogate VLP formation. The VLPs were pleomorphic, exposed protrusions and reacted with patient sera.

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supporting

confidence: 66%

mentioning

confidence: 99%

Hantavirus Gn and Gc Glycoproteins Self-Assemble into Virus-Like Particles

Acuña

Cifuentes-Muñoz

Márquez

et al. 2014

J Virol

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“…Similarly, cryo-electron tomography has enabled clear visualization of rod-like RNPs within Tula (30) and Hantaan (31) viruses, both of the Hantavirus genus. In Hantaan virus, parallel rod-like RNPs ∼10 nm in diameter and up to 100 nm long are observed, the median diameter of the virions being 132 nm (31). On the other hand, RNPs are much less distinctly seen in the interior of two Phleboviruses, Rift Valley Fever (8,32) and Uukuniemi (33).…”

Section: Discussionmentioning

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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“…The spherical hantavirus particles (7) harbor three genomic RNA segments (S, M, and L) within a lipid bilayer (8), encoding viral nucleocapsid protein (N protein), viral RNA-dependent RNA polymerase (RdRp), and glycoprotein precursor (GPC), respectively. The GPC is posttranslationally cleaved at a highly conserved WAASA motif, generating two glycoproteins, Gn and Gc (9). N protein is multifunctional, primarily involved in encapsidation of the viral genome.…”

mentioning

confidence: 99%