Sequence Diversity within the Reovirus S3 Gene: Reoviruses Evolve Independently of Host Species, Geographic Locale, and Date of Isolation

Goral, Mehmet I.; Mochow-Grundy, Michelle; Dermody, Terence S.

doi:10.1006/viro.1996.0059

Cited by 41 publications

(47 citation statements)

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“…Reovirus genomic dsRNA was purified from second-passage L-cell lysate stocks by previously described techniques (15). Oligodeoxynucleotide primers 5Ј-AAGTCACGCCTGTCGTCGTC-3Ј and 5Ј-A CCACCAAGACACCGGCACA-3Ј, which correspond to the 5Ј and 3Ј termini of the S3 gene, respectively, were used to generate cDNA clones from genomic dsRNA.…”

Section: Cells and Virusesmentioning

confidence: 99%

Reovirus ςNS Protein Is Required for Nucleation of Viral Assembly Complexes and Formation of Viral Inclusions

Becker

Goral

Hazelton

et al. 2001

J Virol

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Progeny virions of mammalian reoviruses are assembled in the cytoplasm of infected cells at discrete sites termed viral inclusions. Studies of temperature-sensitive (ts) mutant viruses indicate that nonstructural protein NS and core protein 2 are required for synthesis of double-stranded (ds) RNA, a process that occurs at sites of viral assembly. We used confocal immunofluorescence microscopy and ts mutant reoviruses to define the roles of NS and 2 in viral inclusion formation. In cells infected with wild-type (wt) reovirus, NS and 2 colocalize to large, perinuclear structures that correspond to viral inclusions. In cells infected at a nonpermissive temperature with NS-mutant virus tsE320, NS is distributed diffusely in the cytoplasm and 2 is contained in small, punctate foci that do not resemble viral inclusions. In cells infected at a nonpermissive temperature with 2-mutant virus tsH11.2, 2 is distributed diffusely in the cytoplasm and the nucleus. However, NS localizes to discrete structures in the cytoplasm that contain other viral proteins and are morphologically indistinguishable from viral inclusions seen in cells infected with wt reovirus. Examination of cells infected with wt reovirus over a time course demonstrates that NS precedes 2 in localization to viral inclusions. These findings suggest that viral RNA-protein complexes containing NS nucleate sites of viral replication to which other viral proteins, including 2, are recruited to commence dsRNA synthesis.

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Section: Cells and Virusesmentioning

confidence: 99%

Reovirus ςNS Protein Is Required for Nucleation of Viral Assembly Complexes and Formation of Viral Inclusions

Becker

Goral

Hazelton

et al. 2001

J Virol

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“…All 12 of the 1E1-and 5C6-resistant mutants for which S1 sequences were determined contained these two additional nucleotide changes relative to the published T1L S1 sequences and were thus identical to their parents in that regard. (20,23). The results for reoviruses T1L, T2/simian/Maryland/ SV59/1958 (T2S59), and T3D, evaluated for neutralization by 1E1 in an identical manner, were previously reported (24) and were added to this figure for comparison.…”

Section: Resultsmentioning

confidence: 99%

“…The plaque reduction assay in cell culture is the classical method for demonstrating antibody-mediated neutralization of viral particles (57). We used this assay to test the neutralizing capacity of 1E1 with several additional reovirus isolates (20,23) than previously tested (24) in L929 cells. The results demonstrated that 1E1 neutralizes the two newly tested type 1 isolates, but neither of the two newly tested type 2 isolates nor the two newly tested type 3 isolates (Fig.…”

Section: Resultsmentioning

confidence: 99%

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Protective Immunoglobulin A and G Antibodies Bind to Overlapping Intersubunit Epitopes in the Head Domain of Type 1 Reovirus Adhesin σ1

Helander

Miller

Myers

et al. 2004

J Virol

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Nonfusogenic mammalian orthoreovirus (reovirus) is an enteric pathogen of mice and a useful model for studies of how an enteric virus crosses the mucosal barrier of its host and is subject to control by the mucosal immune system. We recently generated and characterized a new murine immunoglobulin A (IgA)-class monoclonal antibody (MAb), 1E1, that binds to the adhesin fiber, 1, of reovirus type 1 Lang (T1L) and thereby neutralizes the infectivity of that strain in cell culture. 1E1 is produced in hybridoma cultures as a mixture of monomers, dimers, and higher polymers and is protective against peroral challenges with T1L either when the MAb is passively administered or when it is secreted into the intestines of mice bearing subcutaneous hybridoma tumors. In the present study, selection and analysis of mutants resistant to neutralization by 1E1 identified the region of T1L 1 to which the MAb binds. The region bound by a previously characterized type 1 1-specific neutralizing IgG MAb, 5C6, was identified in the same way. Each of the 15 mutants isolated and analyzed was found to be much less sensitive to neutralization by either 1E1 or 5C6, suggesting the two MAbs bind to largely overlapping regions of 1. The tested mutants retained the capacity to recognize specific glycoconjugate receptors on rabbit M cells and cultured epithelial cells, even though viral binding to epithelial cells was inhibited by both MAbs. S1 sequence determinations for 12 of the mutants identified 1 mutations at four positions between residues 415 and 447, which contribute to forming the receptor-binding head domain. When aligned with the 1 sequence of reovirus type 3 Dearing (T3D) and mapped onto the previously reported crystal structure of the T3D 1 trimer, the four positions cluster on the side of the 1 head, across the interface between two subunits. Three such interface-spanning epitopes are thus present per 1 trimer and require the intact quaternary structure of the head domain for MAb binding. Identification of these intersubunit epitopes on 1 opens the way for further studies of the mechanisms of antibody-based neutralization and protection with type 1 reoviruses.

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“…Analysis of the S 1 gene of MRV belonging to different serotypes has shown a strict correlation between sequence similarity and viral serotype [34,56,117]. Conversely, the other genome segments do not display any correlation to viral serotype, suggesting that MRV have evolved independently of serotype in the various species [25,37,71,87,94].…”

Section: Canine Reovirusmentioning

confidence: 99%

Canine respiratory viruses

2007

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-Acute contagious respiratory disease (kennel cough) is commonly described in dogs worldwide. The disease appears to be multifactorial and a number of viral and bacterial pathogens have been reported as potential aetiological agents, including canine parainfluenza virus, canine adenovirus and Bordetella bronchiseptica, as well as mycoplasmas, Streptococcus equi subsp. zooepidemicus, canine herpesvirus and reovirus-1,-2 and -3. Enhancement of pathogenicity by multiple infections can result in more severe clinical forms. In addition, acute respiratory diseases associated with infection by influenza A virus, and group I and II coronaviruses, have been described recently in dogs. Host species shifts and tropism changes are likely responsible for the onset of these new pathogens. The importance of the viral agents in the kennel cough complex is discussed.

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Sequence Diversity within the Reovirus S3 Gene: Reoviruses Evolve Independently of Host Species, Geographic Locale, and Date of Isolation

Cited by 41 publications

References 0 publications

Reovirus ςNS Protein Is Required for Nucleation of Viral Assembly Complexes and Formation of Viral Inclusions

Reovirus ςNS Protein Is Required for Nucleation of Viral Assembly Complexes and Formation of Viral Inclusions

Protective Immunoglobulin A and G Antibodies Bind to Overlapping Intersubunit Epitopes in the Head Domain of Type 1 Reovirus Adhesin σ1

Canine respiratory viruses

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