Molecular characterization and expression of the S3 gene of muscovy duck reovirus strain 89026.

Gall-Recul√©, G Le; Cherbonnel, Martine; Arnauld, C; Blanchard, Philippe; Jestin, André; Jestin, Véronique

doi:10.1099/0022-1317-80-1-195

Cited by 30 publications

(33 citation statements)

References 32 publications

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“…The σ3 protein putative zinc-finger in the CCHC box (amino acid positions 51 to 73) is believed to increase the stability of reoviruses, which has been reported here and in previously published ARV σB sequences (Mabrouk & Lemay, 1994;Le Gall-Recule et al, 1999;Kapczynski et al, 2002;Sellers et al, 2004). The ARV σB protein, like the mammalian reovirus σ3 protein, contains a C-terminal functional domain, which binds dsRNA-binding through a repeated basic amino acid motif (Schiff et al, 1988;Miller & Samuel, 1992;Kapczynski et al, 2002;Sellers et al, 2004)).…”

Section: Discussionsupporting

confidence: 75%

“…The ARV σB protein, like the mammalian reovirus σ3 protein, is composed of two independent functional domains: a zinc-finger motif and a dsRNA binding region (Schiff et al, 1988;Le Gall-Recule et al, 1999). The σ3 protein putative zinc-finger in the CCHC box (amino acid positions 51 to 73) is believed to increase the stability of reoviruses, which has been reported here and in previously published ARV σB sequences (Mabrouk & Lemay, 1994;Le Gall-Recule et al, 1999;Kapczynski et al, 2002;Sellers et al, 2004).…”

Section: Discussionsupporting

confidence: 75%

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Molecular characterization of turkey enteric reovirus S3 gene

et al. 2014

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The molecular diversity in S3 gene sequences of turkey reovirus (TRV) was determined in poult enteritis syndrome (PES)-affected and apparently healthy turkey poults. Twenty-nine TRV-positive samples (15 from PESaffected flocks and 14 from apparently healthy flocks) were tested using self-designed primers for the S3 gene. Phylogenetic analysis revealed that the TRV S3 sequences of this study clustered in clade III and formed two different groups in this clade. The avian reoviruses from duck and goose formed clade I and those from chickens formed clade II. The clade III TRV sequences had a nucleotide percent identity of 88.9 to 100% among themselves but only of 59.5 to 63.5% and 69.2 to 72.6% with clades I and II, respectively. More amino acid substitutions were present in TRVs from PES-affected flocks than in those from apparently healthy flocks using ATCC VR-818 (AY444912) as a benchmark. All TRVs of this study showed substitutions at positions 244 and 285. The impact of these changes on the virulence of the virus, if any, needs to be studied.

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Section: Discussionsupporting

confidence: 75%

Section: Discussionsupporting

confidence: 75%

Molecular characterization of turkey enteric reovirus S3 gene

et al. 2014

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“…The σB is one of the major outer capsid proteins of ARV and is able to induce group-specific neutralizing antibody [15,16]. The precise analysis of the epitopes in σB protein is important for understanding the mechanism of σB-mediated protection.…”

Section: Discussionmentioning

confidence: 99%

“…σB, a major outer capsid protein of ARV, is structurally related to the σ3 protein of mammalian reovirus (MRV) and the σB protein of DRV, which suggests it is a functional protein. The σB protein of ARV comprises 367 amino acids and is able to induce group-specific neutralizing antibodies [15,16]. The σB proteins of the ARV strains contain conserved immunogenic regions, suggesting that the σB protein can potentially be used as a target to raise pan-ARV σB mAbs for the detection of a broad spectrum of avian reoviruses.…”

Section: Introductionmentioning

confidence: 99%

Antigenic Analysis of Monoclonal Antibodies against Different Epitopes of σB Protein of Avian Reovirus

et al. 2013

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BackgroundAvian reovirus (ARV) causes arthritis, tenosynovitis, runting-stunting syndrome (RSS), malabsorption syndrome (MAS) and immunosuppression in chickens. σB is one of the major structural proteins of ARV, which is able to induce group-specific antibodies against the virus.Methods and ResultsThe present study described the identification of two linear B-cell epitopes in ARV σB through expressing a set of partially overlapping and consecutive truncated peptides spanning σB screened with two monoclonal antibodies (mAbs) 1F4 and 1H3-1.The data indicated that 21KTPACW26 (epitope A) and 32WDTVTFH38 (epitope B) were minimal determinants of the linear B cell epitopes. Antibodies present in the serum of ARV-positive chickens recognized the minimal linear epitopes in Western blot analyses. By sequence alignment analysis, we determined that the epitopes A and B were not conserved among ARV, duck reovirus (DRV) and turkey reovirus (TRV) strains. Western blot assays, confirmed that epitopes A and B were ARV-specific epitopes, and they could not react with the corresponding peptides of DRV and TRV.Conclusions and SignificanceWe identified 21KTPACW26 and 32WDTVTFH38 as σB -specific epitopes recognized by mAbs 1F4 and 1H3-1, respectively. The results in this study may have potential applications in development of diagnostic techniques and epitope-based marker vaccines against ARV groups.

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“…The σB protein of DRV encoded by S3 gene segment is structurally related to the σ3 protein of mammalian or σB of ARV [9-12] and may be functional related. The σB protein is a major constituent of the outer capsid and, like σC, is exposed to the surface of the virion [2].…”

Section: Introductionmentioning

confidence: 99%

Characterization of monoclonal antibodies against Muscovy duck reovirus σB protein

Liu

Chen

Wang

et al. 2010

Virol J

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BackgroundThe σB protein of Muscovy duck reovirus (DRV), one of the major structural proteins, is able to induce neutralizing antibody in ducks, but the monoclonal antibody (MAb) against σB protein has never been characterized.ResultsFour hybridoma cell lines secreting anti-DRV σB MAbs were obtained, designated 1E5, 2F7, 4E3 and 5D8. Immunoglobulin subclass tests differentiated them as IgG2b (1E5 and 4E3) and IgM (2F7 and 5D8). Dot blot and western blotting assays showed that MAbs reacted with His-σB protein in a conformation-independent manner. Competitive binding assay indicated that the MAbs delineated two epitopes, A and B of σB. Immunofluorescence assay indicated that the four MAbs could specifically bind to Vero cells infected with DRV and σB was distributed diffusely in the cytoplasma of infected cells. MAbs had universal reactivity to all DRVs tested in an antigen-capture enzyme-linked immunosorbent assay.ConclusionResults of this research provide important information about the four monoclonal antibodies and therefore the MAbs may be useful candidate for the development of a MAb capture ELISA for rapid detection of DRVs. In addition, it showed that the σB protein was located in the cytoplasma of infected cells by immunofluorescence assay with MAbs. Virus isolation and RT-PCR are reliable way for detection of DRV infection, but these procedures are laborious, time consuming, and requiring instruments. These obvious diagnosis problems highlight the ongoing demand of rapid, reproducible, and automatic methods for the sensitive detection of DRV.

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Molecular characterization and expression of the S3 gene of muscovy duck reovirus strain 89026.

Cited by 30 publications

References 32 publications

Molecular characterization of turkey enteric reovirus S3 gene

Molecular characterization of turkey enteric reovirus S3 gene

Antigenic Analysis of Monoclonal Antibodies against Different Epitopes of σB Protein of Avian Reovirus

Characterization of monoclonal antibodies against Muscovy duck reovirus σB protein

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