Reptilian reovirus: a new fusogenic orthoreovirus species

Duncan, Roy; Corcoran, Jennifer A.; Shou, Jingyun; Stoltz, Donald B.

doi:10.1016/j.virol.2003.10.025

Cited by 62 publications

(64 citation statements)

References 42 publications

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“…Sequence analysis of the four small (S) segments indicated a very close genetic relationship between the two viruses. One S class genome segment of orthoreoviruses may be polycistronic, and its coding arrangement is characteristic of a particular species group (24). As shown in Fig.…”

Section: Molecular and Phylogenetic Characterizationmentioning

confidence: 99%

A previously unknown reovirus of bat origin is associated with an acute respiratory disease in humans

Chua

Crameri

Hyatt

et al. 2007

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

204

259

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Respiratory infections constitute the most widespread human infectious disease, and a substantial proportion of them are caused by unknown etiological agents. Reoviruses (respiratory enteric orphan viruses) were first isolated from humans in the early 1950s and so named because they were not associated with any known disease. Here, we report a previously unknown reovirus (named ''Melaka virus'') isolated from a 39-year-old male patient in Melaka, Malaysia, who was suffering from high fever and acute respiratory disease at the time of virus isolation. Two of his family members developed similar symptoms Ϸ1 week later and had serological evidence of infection with the same virus. Epidemiological tracing revealed that the family was exposed to a bat in the house Ϸ1 week before the onset of the father's clinical symptoms. Genome sequence analysis indicated a close genetic relationship between Melaka virus and Pulau virus, a reovirus isolated in 1999 from fruit bats in Tioman Island, Malaysia. Screening of sera collected from human volunteers on the island revealed that 14 of 109 (13%) were positive for both Pulau and Melaka viruses. This is the first report of an orthoreovirus in association with acute human respiratory diseases. Melaka virus is serologically not related to the different types of mammalian reoviruses that were known to infect humans asymptomatically. These data indicate that batborne reoviruses can be transmitted to and cause clinical diseases in humans.respiratory infection ͉ zoonosis ͉ human-to-human transmission ͉ orthoreovirus ͉ Pulau virus

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Section: Molecular and Phylogenetic Characterizationmentioning

confidence: 99%

A previously unknown reovirus of bat origin is associated with an acute respiratory disease in humans

Chua

Crameri

Hyatt

et al. 2007

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

204

259

View full text Add to dashboard Cite

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“…The genome comprises ten segments being divided into three classes based on size, including four small (s), three medium (m) and three large (l) segments. The majority of these segments encode one protein; however, the s1 segment across various species can encode up to three proteins (Duncan et al, 2004;Knipe & Howley, 2007).…”

Section: Introductionmentioning

confidence: 99%

Mouse fibroblast L929 cells are less permissive to infection by Nelson Bay orthoreovirus compared to other mammalian cell lines

Mok

Wynne

Grimley

et al. 2015

Journal of General Virology

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In recent years, bats have been identified as a natural reservoir for a diverse range of viruses. Nelson Bay orthoreovirus (NBV) was first isolated from the heart blood of a fruit bat (Pteropus poliocephalus) in 1968. While the pathogenesis of NBV remains unknown, other related members of this group have caused acute respiratory disease in humans. Thus the potential for NBV to impact human health appears plausible. Here, to increase our knowledge of NBV, we examined the replication and infectivity of NBV using different mammalian cell lines derived from bat, human, mouse and monkey. All cell lines supported the replication of NBV; however, L929 cells showed a greater than 2 log reduction in virus titre compared with the other cell lines. Furthermore, NBV did not induce major cytopathic effects in the L929 cells, as was observed in other cell lines. Interestingly, the related Pteropine orthoreoviruses, Pulau virus (PulV) and Melaka virus (MelV) were able to replicate to high titres in L929 cells but infection resulted in reduced cytopathic effect. Our study demonstrates a unique virus-host interaction between NBV and L929 cells, where cells effectively control viral infection/replication and limit the formation of syncytia. By elucidating the molecular mechanisms that control this unique relationship, important insights will be made into the biology of this fusogenic virus.

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“…Although many nonenveloped viruses encode proteins involved in membrane permeabilization (5-7), some of which can induce low levels of cell-to-cell fusion (8), the FAST proteins are the only known examples of nonenveloped virus proteins that evolved specifically to induce cell-to-cell fusion (9). In contrast to the enveloped virus fusion proteins, which are structural proteins that have evolved primarily to mediate virus-cell fusion, the FAST proteins are nonstructural proteins and therefore are not involved in virus entry (10).…”

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confidence: 99%

Features of a Spatially Constrained Cystine Loop in the p10 FAST Protein Ectodomain Define a New Class of Viral Fusion Peptides

Barry¹,

Key²,

Haddad³

et al. 2010

Journal of Biological Chemistry

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The reovirus fusion-associated small transmembrane (FAST) proteins are the smallest known viral membrane fusion proteins. With ectodomains of only ϳ20 -40 residues, it is unclear how such diminutive fusion proteins can mediate cell-cell fusion and syncytium formation. Contained within the 40-residue ectodomain of the p10 FAST protein resides an 11-residue sequence of moderately apolar residues, termed the hydrophobic patch (HP). Previous studies indicate the p10 HP shares operational features with the fusion peptide motifs found within the enveloped virus membrane fusion proteins. Using biotinylation assays, we now report that two highly conserved cysteine residues flanking the p10 HP form an essential intramolecular disulfide bond to create a cystine loop. Mutagenic analyses revealed that both formation of the cystine loop and p10 membrane fusion activity are highly sensitive to changes in the size and spatial arrangement of amino acids within the loop. The p10 cystine loop may therefore function as a cystine noose, where fusion peptide activity is dependent on structural constraints within the noose that force solvent exposure of key hydrophobic residues. Moreover, inhibitors of cell surface thioreductase activity indicate that disruption of the disulfide bridge is important for p10-mediated membrane fusion. This is the first example of a viral fusion peptide composed of a small, spatially constrained cystine loop whose function is dependent on altered loop formation, and it suggests the p10 cystine loop represents a new class of viral fusion peptides.Membrane fusion is an essential process involved in an abundance of biological events, including sperm-egg fusion, multinucleated myotube formation, exocytosis, and enveloped virus entry (1). The fusion reaction is catalyzed by specialized membrane fusion proteins designed to alter bilayer structure and bring about membrane merger. The membrane fusion proteins of various enveloped viruses represent some of the best characterized examples of such fusion catalysts (2). Detailed structural and functional analysis of diverse enveloped virus membrane fusion proteins reveals a common pathway of protein-mediated membrane fusion. Triggered exposure of a hydrophobic fusion peptide (FP), 3 normally sequestered within the complex pre-fusion ectodomain structure of these proteins, results in FP insertion into the donor and/or target membranes. Subsequent structural remodeling of these large ectodomains generates a trimeric hairpin structure that draws the two membranes together, driving lipid mixing (also referred to as hemifusion) and pore formation and expansion (3, 4). Despite a wealth of information, the precise mechanisms by which FPs and conformational remodeling of enveloped virus fusion proteins mediate lipid bilayer rearrangement and fusion remain unclear.The reovirus fusion-associated small transmembrane (FAST) proteins are a singular family of viral membrane fusion proteins. Although many nonenveloped viruses encode proteins involved in membrane permeabilization (...

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Reptilian reovirus: a new fusogenic orthoreovirus species

Cited by 62 publications

References 42 publications

A previously unknown reovirus of bat origin is associated with an acute respiratory disease in humans

A previously unknown reovirus of bat origin is associated with an acute respiratory disease in humans

Mouse fibroblast L929 cells are less permissive to infection by Nelson Bay orthoreovirus compared to other mammalian cell lines

Features of a Spatially Constrained Cystine Loop in the p10 FAST Protein Ectodomain Define a New Class of Viral Fusion Peptides

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