Avian Reovirus Proteins Associated with Neutralization of Virus Infectivity

Wickramasinghe, Ranjit; Meanger, Jayesh; Enrı́quez, Carlos; Wilcox, G. E.

doi:10.1006/viro.1993.1309

Cited by 126 publications

(78 citation statements)

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“…Based on location in the virion, coding assignment to the S1 segment and being the target for type-specific neutralizing antibodies, it has been suggested that avian reovirus a3 protein is analogous to mammalian reovirus al attachment protein (Schnitzer et al, 1982;Schnitzer, 1985;Wickramasinghe et al, 1993;Varela & Benavente, 1994;Menager et al, 1995;Shapouri et al, 1996). In agreement with this suggestion, sequence analysis of avian reovirus S 1 segment (Shapouri et al, 1995) revealed the presence of a heptad repeat region previously reported for mammalian o-1 (Bassel-Duby et al, 1985;Duncan et al, 1990), in the N-terminal half of o-3 protein.…”

Section: Discussionmentioning

confidence: 99%

“…It has thus far been hypothesized that a3, also known as a c (Schnitzer et al, 1982), is the virus attachment protein. This hypothesis was based on the analogy of this protein with al, the mammalian reovirus attachment protein, with respect to localization at the virion surface (Schnitzer et al, 1982), determination of its coding assignment to S1 genome segment (Schnitzer, 1985;Varela & Benavente, 1994) and its association with type-specific neutralization of the virus (Wickramasinghe et al, 1993 ;Menager et al, 1995;Shapouri et al, 1996). *Author for correspondence.…”

Section: Introductionmentioning

confidence: 99%

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Evidence for the multimeric nature and cell binding ability of avian reovirus 3 protein

Shapouri

Arella²,

Silim³

1996

Journal of General Virology

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It has been suggested that avian reovirus ¢r3 protein is analogous to al trimer, the mammalian reovirus attachment protein. We have investigated the multimeric nature and cell binding ability of a3 protein.The data presented here demonstrate that a3 protein is a multimer in its undisrupted form as determined by SDS-PAGE in non-dissociating conditions. However, virion-associated a3 protein and COS-7 cell-expressed protein behaved differently in SDS-PAGE, suggesting a need for virusassociated factor(s) to control the multimerization of the protein. The data also show that Escherichia coil expressed o'3 fusion protein (~r3-MBP) in its multimeric form is capable of attaching to Vero cells. The binding was found to be specific and receptor mediated by the fact that it was inhibited by a monoclonal antibody specific for a3 protein and by competition with avian reovirus particles. As determined by a reverse experiment, tr3-MBP was also able to reduce the virus p.f.u. in monolayer cell cultures, indicating the important role of a3 protein in the initiation of virus infection.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Evidence for the multimeric nature and cell binding ability of avian reovirus 3 protein

Shapouri

Arella²,

Silim³

1996

Journal of General Virology

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“…Various serological diagnostic techniques have been developed for efficient detection of antibodies against ARV, including serum neutralization test (Wickramasinghe et al, 1993), AGID (Meanger et al, 1995), immunoblot assay (Ide and Dewitt, 1979) and ELISA (Liu et al, 2002). Several indirect ELISA diagnostic test based on recombinant σC and σB protein have been developed and validated for detection of antibodies against ARV (Zhang et al, 2007).…”

Section: Issn: 2319-7706 Volume 6 Number 9 (2017) Pp 434-441mentioning

confidence: 99%

High-Yield Expression and Purification of Recombinant σB Protein of Avian Reovirus (ARV) in Prokaryotic System

Kamble¹,

Mohan²,

Dey³

2017

Int.J.Curr.Microbiol.App.Sci

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“…The σC (sigma C) protein of ARV, which is analogous to the σ1 (sigma 1) protein of MRV, has been reported to be the virus attachment protein (Martinez-Costas et al, 1997). It is the target for type-specific neutralizing antibodies (Wickramasinghe et al, 1993). Since the natural hosts for ARVs are various avian species (Rosenberger, 2003); mammals including humans and domestic animals could be expected to be seronegative to ARV.…”

Section: Introductionmentioning

confidence: 99%

Anti-neoplastic effect of avian reovirus σ C protein on Rous sarcoma virus-induced tumors in chicken

Uma¹,

Kataria²,

Rahul³

et al. 2013

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Summary. -This study investigated the anti-neoplastic potential of avian reovirus σC (sigma C) protein on Rous sarcoma virus-induced fibrosarcoma in chicken. The recombinant vector expressing σC protein was injected intra-tumorally into specific pathogen free chicken with fibro-sarcoma at the dose 100µg per bird, while control birds were mock-treated with 100µg of empty vector per bird. Recombinant σC protein induced apoptosis in tumors of treated birds resulting in progressive tumor regression, while similar changes were absent in tumors of mock-treated controls. The σC protein-induced apoptosis in tumors was quantified by flow cytometry and the mean level of apoptosis up to 66% was observed in treated tumors, whereas any significant level of apoptosis was absent in mock-treated controls.Keywords: avian reovirus; Rous sarcoma virus; tumors; σC protein; apoptosis E-mail: uma@kvasu.ac.in; phone: +91-487-2370344-275. Abbreviations: ARV(s) = avian reovirus(es); AO/EtBr = acridine orange/ethidium bromide; CEF = chicken embryonic fibroblast; H&E = hematoxylin and eosin; MRV = mammalian reovirus; MAb = monoclonal antibody; σC = sigma C, σ1 = sigma 1; SPF = specific pathogen free; RSV = Rous sarcoma virus

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Avian Reovirus Proteins Associated with Neutralization of Virus Infectivity

Cited by 126 publications

References 0 publications

Evidence for the multimeric nature and cell binding ability of avian reovirus 3 protein

Evidence for the multimeric nature and cell binding ability of avian reovirus 3 protein

High-Yield Expression and Purification of Recombinant σB Protein of Avian Reovirus (ARV) in Prokaryotic System

Anti-neoplastic effect of avian reovirus σ C protein on Rous sarcoma virus-induced tumors in chicken

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