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Ananta K. Ghosh - One of the best experts on this subject based on the ideXlab platform.
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Genome segment 5 of Antheraea mylitta cytoplasmic polyhedrosis virus encodes a bona fide guanylyltransferase
Virology Journal, 2014Co-Authors: Poulomi Biswas, Anirban Kundu, Ananta K. GhoshAbstract:Background Antheraea mylitta cytoplasmic polyhedrosis virus (AmCPV), a Cypovirus of Reoviridae family, infects non mulberry Indian silk worm, Antheraea mylitta, and contains eleven segmented double stranded RNA in its genome (S1-S11). Some of its genome segments (S1-S3, and S6-S11) have been previously characterized but genome segment encoding the viral guanylyltransferase which helps in RNA capping has not been characterized.
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Molecular characterization of genome segments 1 and 3 encoding two capsid proteins of Antheraea mylitta cytoplasmic polyhedrosis virus
Virology Journal, 2010Co-Authors: Mrinmay Chakrabarti, Suvankar Ghorai, Saravana Kk Mani, Ananta K. GhoshAbstract:Background Antheraea mylitta cytoplasmic polyhedrosis virus (AmCPV), a Cypovirus of Reoviridae family, infects Indian non-mulberry silkworm, Antheraea mylitta, and contains 11 segmented double stranded RNA (S1-S11) in its genome. Some of its genome segments (S2 and S6-S11) have been previously characterized but genome segments encoding viral capsid have not been characterized.
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Molecular characterization of genome segments 1 and 3 encoding two capsid proteins of Antheraea mylittacytoplasmic polyhedrosis virus
Virology Journal, 2010Co-Authors: Mrinmay Chakrabarti, Suvankar Ghorai, Saravana Kk Mani, Ananta K. GhoshAbstract:Background Antheraea mylitta cytoplasmic polyhedrosis virus (AmCPV), a Cypovirus of Reoviridae family, infects Indian non-mulberry silkworm, Antheraea mylitta , and contains 11 segmented double stranded RNA (S1-S11) in its genome. Some of its genome segments (S2 and S6-S11) have been previously characterized but genome segments encoding viral capsid have not been characterized. Results In this study genome segments 1 (S1) and 3 (S3) of AmCPV were converted to cDNA, cloned and sequenced. S1 consisted of 3852 nucleotides, with one long ORF of 3735 nucleotides and could encode a protein of 1245 amino acids with molecular mass of ~141 kDa. Similarly, S3 consisted of 3784 nucleotides having a long ORF of 3630 nucleotides and could encode a protein of 1210 amino acids with molecular mass of ~137 kDa. BLAST analysis showed 20-22% homology of S1 and S3 sequence with spike and capsid proteins, respectively, of other closely related Cypoviruses like Bombyx mori CPV (BmCPV), Lymantria dispar CPV (LdCPV), and Dendrolimus punctatus CPV (DpCPV). The ORFs of S1 and S3 were expressed as 141 kDa and 137 kDa insoluble His-tagged fusion proteins, respectively, in Escherichia coli M15 cells via pQE-30 vector, purified through Ni-NTA chromatography and polyclonal antibodies were raised. Immunoblot analysis of purified polyhedra, virion particles and virus infected mid-gut cells with the raised anti-p137 and anti-p141 antibodies showed specific immunoreactive bands and suggest that S1 and S3 may code for viral structural proteins. Expression of S1 and S3 ORFs in insect cells via baculovirus recombinants showed to produce viral like particles (VLPs) by transmission electron microscopy. Immunogold staining showed that S3 encoded proteins self assembled to form viral outer capsid and VLPs maintained their stability at different pH in presence of S1 encoded protein. Conclusion Our results of cloning, sequencing and functional analysis of AmCPV S1 and S3 indicate that S3 encoded viral structural proteins can self assemble to form viral outer capsid and S1 encoded protein remains associated with it as inner capsid to maintain the stability. Further studies will help to understand the molecular mechanism of capsid formation during Cypovirus replication.
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Molecular characterization of genome segment 2 encoding RNA dependent RNA polymerase of Antheraea mylitta cytoplasmic polyhedrosis virus
Virology, 2010Co-Authors: Suvankar Ghorai, Mrinmay Chakrabarti, Venkata R M Chavali, Abhisek Bagchi, Ananta K. GhoshAbstract:Abstract Genome segment 2 (S2) from Antheraea mylitta Cypovirus (AmCPV) was converted into cDNA, cloned and sequenced. S2 consisted of 3798 nucleotides with a long ORF encoding a 1116 amino acid long protein (123 kDa). BLAST and phylogenetic analysis showed 29% sequence identity and close relatedness of AmCPV S2 with RNA dependent RNA polymerase (RdRp) of other insect Cypoviruses, suggesting a common origin of all insect Cypoviruses. The ORF of S2 was expressed as 123 kDa soluble His-tagged fusion protein in insect cells via baculovirus recombinants which exhibited RdRp activity in an in vitro RNA polymerase assay without any intrinsic terminal transferase activity. Maximum activity was observed at 37 °C at pH 6.0 in the presence of 3 mM MgCl 2. Site directed mutagenesis confirmed the importance of the conserved GDD motif. This is the first report of functional characterization of a cypoviral RdRp which may lead to the development of anti-viral agents.
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genome segment 6 of antheraea mylitta Cypovirus encodes a structural protein with atpase activity
Virology, 2008Co-Authors: Venkata R M Chavali, Suvankar Ghorai, Chaithanya Madhurantakam, Ananta K. GhoshAbstract:The genome segment 6 (S6) of the 11 double stranded RNA genomes from Antheraea mylitta Cypovirus was converted into cDNA, cloned and sequenced. S6 consisted of 1944 nucleotides with an ORF of 607 amino acids and could encode a protein of 68 kDa, termed P68. Motif scan and molecular docking analysis of P68 showed the presence of two cystathionine beta synthase (CBS) domains and ATP binding sites. The ORF of AmCPV S6 was expressed in E. coli as His-tag fusion protein and polyclonal antibody was raised. Immunoblot analysis of virus infected gut cells and purified polyhedra using raised anti-p68 polyclonal antibody showed that S6 encodes a viral structural protein. Fluorescence and ATPase assay of soluble P68 produced in Sf-9 cells via baculovirus expression system showed its ability to bind and cleave ATP. These results suggest that P68 may bind viral RNA through CBS domains and help in replication and transcription through ATP binding and hydrolysis.
G. R. Carner - One of the best experts on this subject based on the ideXlab platform.
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molecular and biological characterization of a Cypovirus from the mosquito culex restuans
Journal of Invertebrate Pathology, 2006Co-Authors: Terry B Green, G. R. Carner, Peter P. C. Mertens, Alexandra M Shapiro, Susan E White, James J BecnelAbstract:A Cypovirus from the mosquito Culex restuans (named CrCPV) was isolated and its biology, morphology, and molecular characteristics were investigated. CrCPV is characterized by small (0.1–1.0m), irregularly shaped inclusion bodies that are multiply embedded. Laboratory studies demonstrated that divalent cations inXuenced transmission of CrCPV to Culex quinquefasciatus larvae; magnesium enhanced CrCPV transmission by »30% while calcium inhibited transmission. CrCPV is the second Cypovirus from a mosquito that has been conWrmed by using molecular analysis. CrCPV has a genome composed of 10 dsRNA segments with an electropherotype similar to the recently discovered UsCPV-17 from the mosquito Uranotaenia sapphirina, but distinct from the lepidopteran Cypoviruses BmCPV-1 (Bombyx mori) and TnCPV-15 (Trichoplusia ni). Nucleotide and deduced amino acid sequence analysis of CrCPV segment 10 (polyhedrin) suggests that CrCPV is closely related (83% nucleotide sequence identity and 87% amino acid sequence identity) to the newly characterized UsCPV-17 but is unrelated to the 16 remaining CPV species from lepidopteran hosts. A comparison of the terminal segment regions of CrCPV and UsCPV-17, an additional method for diVerentiating various Cypovirus species, revealed a high level of conservation. Therefore, we propose that CrCPV is a member of the Cypovirus-17 group and designate this species as CrCPV-17.
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morphological and molecular characterization of a Cypovirus reoviridae from the mosquito uranotaenia sapphirina diptera culicidae
Journal of Virology, 2005Co-Authors: Alexandra M Shapiro, G. R. Carner, Peter P. C. Mertens, Terry B Green, Susan E White, James J BecnelAbstract:The first report of an occluded cytoplasmic insect virus was from the midgut epithelial cells of the silkworm Bombyx mori (16). The virus was subsequently identified as a cytoplasmic polyhedrosis virus (CPV) to distinguish it from the nuclear polyhedrosis viruses already recognized (27). CPVs are commonly isolated from insects, mainly from Lepidoptera and occasionally from Diptera or Hymenoptera, but only rarely from Coleoptera or Neuroptera (15). Cytoplasmic polyhedrosis viruses usually have a ten-segmented double-stranded RNA (dsRNA) genome and are classified as members of the genus Cypovirus within the family Reoviridae (14, 20). Different Cypovirus “types” were initially identified on the basis of differences in the migration patterns of their genome segments during polyacrylamide gel electrophoresis, i.e., electropherotypes (22). Subsequent studies showed a good correlation between electropherotype and the grouping of strains on the basis of serological properties (18) or RNA cross-hybridization (17, 20). It has recently been shown that, in addition to the RNA migration patterns, nucleotide sequences, for example, those of genome segment 10 (Seg-10; the polyhedrin gene), can be used to distinguish different Cypovirus species (20). Sixteen Cypovirus species (types) are currently recognized, all from lepidopteran hosts (20). Numerous viruses (isolated before the recognition of the genus Cypovirus) from the larvae of 20 different species of mosquitoes (representing nine different genera) were identified as CPVs based on similarities to viruses from Lepidoptera (12). These similarities included virion structure, the presence of inclusion bodies (polyhedra), and chronic infection in the cytoplasm of midgut epithelial cells. There were also three reports of CPVs from the midgut epithelium of adult mosquitoes (7, 8, 11). However, there was no further biophysical or biochemical analyses of these mosquito Cypoviruses. We report an analysis of the biology, morphology, and molecular characteristics of a new CPV isolate from the mosquito Uranotaenia sapphirina (UsCPV). The data generated demonstrate that UsCPV has a distinct electropherotype and represents a new Cypovirus species.
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Comparison of the amino acid sequences of RNA-dependent RNA polymerases of Cypoviruses in the family Reoviridae ^*
Archives of Virology, 2003Co-Authors: G. R. Carner, S. W. Scott, T. Omura, K. HagiwaraAbstract:The nucleotide sequences of the genome segment S2 of Bombyx mori Cypovirus 1, S2 of Lymantria dispar Cypovirus 1, S1 of Lymantria dispar Cypovirus 14 and S1 of a proposed new electropherotype of Trichoplusia ni Cypovirus 15 were determined. These segments encoded putative RNA-dependent RNA polymerases (RDRPs). The deduced amino acid sequences of RDRPs within the genus Cypovirus showed 32% to 94% identities, while extent of homology between RDRPs in the genera Cypovirus and Oryzavirus , a genus most closely related, was approximately 26% identity. Both the genera Cypovirus and Oryzavirus might have originated from a common insect virus ancestor.
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nucleotide sequences of segments 1 3 and 4 of the genome of bombyx mori Cypovirus 1 encoding putative capsid proteins vp1 vp3 and vp4 respectively
Journal of General Virology, 2002Co-Authors: Kyoji Hagiwara, S. W. Scott, G. R. CarnerAbstract:The complete nucleotide sequences of genomic segments S1, S3 and S4 from Bombyx mori Cypovirus 1 (BmCPV-1) have been determined. The segments consisted of 4190, 3846 and 3262 nucleotides encoding putative proteins of 1333, 1239 and 1058 amino acids with molecular masses of approximately 148, 140 and 120 kDa (p148, p140 and p120, respectively). All segments possess a single open reading frame. Homology searches showed that all three proteins have homologies to proteins of Rice ragged stunt virus, a member of the genus Oryzavirus within the family Reoviridae. Partial homologies of p140 to structural proteins in other viruses were also found. The predicted molecular masses and the homologies with structural proteins in other viruses lead us to suggest that S1, S3 and S4 encode the capsid proteins VP1, VP3, and VP4, respectively, of BmCPV-1.
H. Y. Peng - One of the best experts on this subject based on the ideXlab platform.
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Characterization of the RNA-binding domain in the Dendrolimus punctatus cytoplasmic polyhedrosis virus nonstructural protein p44.
Virus research, 2005Co-Authors: S.l. Zhao, C. Y. Liang, W J Zhang, X C Tang, H. Y. PengAbstract:Dendrolimus punctatus cytoplasmic polyhedrosis virus (DpCPV-1) belongs to the Cypovirus genus in the Reoviridae family. The ORF of genome segment 8 (S8) of DpCPV-1 was cloned into vector pMAL-c2X and used to express a 44kDa protein (p44) in E. coli, which was detected by Western blotting. The gel mobility shift assays showed that p44 had ssRNA-binding activity. Competitive assay indicated that this protein only bind to ssRNA and could not interact with DNA and dsRNA. The binding of p44 to ssRNA is sequence non-specific. To identify the domain(s) important for RNA binding of the protein, a number of deletions were made. These truncated proteins were expressed in E. coli and purified. The affinity of each truncated protein towards ssRNA was then assayed by electrophoretic mobility shift assays and northwestern blot. The results indicated that glutamic acid-rich domain in the central region of p44 from residues 104 to 201 was the ssRNA-binding domain.
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Nucleotide sequences of genome segments S6, S7 and S10 of Dendrolimus punctatus Cypovirus 1 ∗
Archives of Virology, 2003Co-Authors: Jingjun Hong, S.l. Zhao, J. L. Duan, Hua Xu, H. Y. PengAbstract:The nucleotide sequences of genome segments S6, S7 and S10 of Dendrolimus punctatus Cypovirus 1 Hunan I (DpCPV-HN(I)) and DpCPV-HN(I)-Se3 (DpCPV-HN(I) passed three times in Spodoptera exigua) were determined. Segment S10 was 944 nucleotides in length and encoded a polyhedrin of 248 amino acids (28 439 Da). Only two nucleotide mutations were found between DpCPV-HN(I) S10 and DpCPV-HN(I)-Se3 S10, and the deduced amino acid sequences of the polyhedrin proteins were identical. Segment S7, 1 501 nucleotides, encoded a protein of 448 amino acids (∼50 kDa; p50). Thirty-one nucleotide mutations were found between DpCPV-HN(I) S7 and DpCPV-HN(I)-Se3 S7, but these resulted in only four amino acid changes. DpCPV-HN(I) S6 encoded a protein of 561 amino acids (63 688 Da; p64). The amino acid sequence of p64, had a high leucine content (10%), and contained a leucine zipper motif and one ATP/GTP-binding site motif.
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Nucleotide sequences of genome segments S6, S7 and S10 of Dendrolimus punctatus Cypovirus 1
Archives of Virology, 2003Co-Authors: J. J. Hong, S.l. Zhao, H.g. Xu, J. L. Duan, H. Y. PengAbstract:The nucleotide sequences of genome segments S6, S7 and S10 of Dendrolimus punctatus Cypovirus 1 Hunan I (DpCPV-HN(I)) and DpCPV-HN(I)-Se_3 (DpCPV-HN(I) passed three times in Spodoptera exigua ) were determined. Segment S10 was 944 nucleotides in length and encoded a polyhedrin of 248 amino acids (28 439 Da). Only two nucleotide mutations were found between DpCPV-HN(I) S10 and DpCPV-HN(I)-Se_3 S10, and the deduced amino acid sequences of the polyhedrin proteins were identical. Segment S7, 1 501 nucleotides, encoded a protein of 448 amino acids (∼50 kDa; p50). Thirty-one nucleotide mutations were found between DpCPV-HN(I) S7 and DpCPV-HN(I)-Se_3 S7, but these resulted in only four amino acid changes. DpCPV-HN(I) S6 encoded a protein of 561 amino acids (63 688 Da; p64). The amino acid sequence of p64, had a high leucine content (10%), and contained a leucine zipper motif and one ATP/GTP-binding site motif.
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Genomic sequence analyses of segments 1 to 6 of Dendrolimus punctatus cytoplasmic polyhedrosis virus
Archives of Virology, 2003Co-Authors: S.l. Zhao, C. Y. Liang, J. J. Hong, H. Y. PengAbstract:The complete nucleotide sequences of genomic segments S1 to S6 from Dendrolimus punctatus Cypovirus 1 (DpCPV-1) have been determined. Each segment of S1 to S6 posses a single open reading frame. Conserved motifs 5′ (AGUAA) and 3′(GUUAGCC) were found at the ends of each segment. Comparison of the proteins of DpCPV with those of other members in the family Reoviridae lead us to suggest that S1, S3, S4 and S6 encode the viral structural protein VP1, VP2, VP3 and VP4, respectively. S5 encoded viral non-structural protein p100 and S2 encodes an RNA-dependent RNA polymerase (RdRp). Motif analysis shows that VP3 is similar to the methyltransferase of Methanosarcina mazei Goe1, VP4 has motifs for leucine zipper and ATP/GTP-binding sites, and p100 is remarkably similar to foot-and-mouth disease virus 2A protease (FMDV 2A^pro). Phylogenetic analysis of RdRps from nine viruses of the family Reoviridae indicates that DpCPV is a type 1 Cypovirus, more related to Bombyx mori Cypovirus (BmCPV) than to other Cypovirus species. DpCPV is more related to Rice ragged stunt virus (RRSV) than to other members of different genera of the family Reoviridae , which seems to confirm the previous hypothesis that plant reoviruses originated from insect reoviruses.
James J Becnel - One of the best experts on this subject based on the ideXlab platform.
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Mosquito pathogenic viruses--the last 20 years.
Journal of the American Mosquito Control Association, 2020Co-Authors: James J Becnel, Susan E WhiteAbstract:There are several types of viral pathogens that cause disease in mosquitoes with most belonging to 4 major groups. The most common viruses of mosquitoes are the baculoviruses (NPVs) (Baculoviridae: Nucleopolyhedrovirus) and cytoplasmic polyhedrosis viruses (CPVs) (Reoviridae: Cypovirus). The other major types of viruses in mosquitoes are represented by the densoviruses (DNVs) (Parvoviridae: Brevidensovirus) and the iridoviruses (MIVs) (Iridoviridae: Chloriridovirus). Baculoviruses, densoviruses and iridoviruses are DNA viruses while Cypoviruses are the main RNA viruses in mosquitoes. This chapter presents an overview of the recent advancements in the study of mosquito pathogenic viruses and discusses how this new understanding of virus-mosquito interactions can be used to develop novel research and control strategies.
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Current status of Deltabaculoviruses, Cypoviruses and Chloriridoviruses pathogenic for mosquitoes
Virologica Sinica, 2008Co-Authors: James J BecnelAbstract:There are a variety of viral pathogens that cause disease in mosquitoes with most belonging to three major groups. The most common viruses of mosquitoes are the baculoviruses (DBVs) (Baculoviridae: Deltabaculovirus), cytoplasmic polyhedrosis viruses (CPVs) (Reoviridae: Cypovirus) and the iridoviruses (MIVs) (Iridoviridae: Chloriridovirus). Baculoviruses and iridoviruses are DNA viruses while Cypoviruses are the main RNA viruses in mosquitoes. This review presents an overview of the current status and recent advancements in understanding the biology and molecular features of mosquito pathogenic viruses.
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MOSQUITO PATHOGENIC VIRUSES—THE LAST 20 YEARS
Journal of The American Mosquito Control Association, 2007Co-Authors: James J Becnel, Susan E WhiteAbstract:There are several types of viral pathogens that cause disease in mosquitoes with most belonging to 4 major groups. The most common viruses of mosquitoes are the baculoviruses (NPVs) (Baculoviridae: Nucleopolyhedrovirus) and cytoplasmic polyhedrosis viruses (CPVs) (Reoviridae: Cypovirus). The other major types of viruses in mosquitoes are represented by the densoviruses (DNVs) (Parvoviridae: Brevidensovirus) and the iridoviruses (MIVs) (Iridoviridae: Chloriridovirus). Baculoviruses, densoviruses and iridoviruses are DNA viruses while Cypoviruses are the main RNA viruses in mosquitoes. This chapter presents an overview of the recent advancements in the study of mosquito pathogenic viruses and discusses how this new understanding of virus-mosquito interactions can be used to develop novel research and control strategies.
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biological and molecular studies of a Cypovirus from the black fly simulium ubiquitum diptera simuliidae
Journal of Invertebrate Pathology, 2007Co-Authors: Terry B Green, Peter P. C. Mertens, Susan E White, Peter H Adler, James J BecnelAbstract:A Cypovirus from the black fly Simulium ubiquitum (SuCPV) was isolated and examined using biological and molecular techniques. SuCPV produces small (typically 0.25 μm), polyhedral shaped inclusion bodies (polyhedra), in which the virus particles become multiply embedded. SuCPV is the third Cypovirus isolated from Diptera, but the first from Simuliidae that has been characterized using molecular analyses. SuCPV has a genome composed of 10 segments of dsRNA, with an electrophoretic migration pattern that is different from those of recent UsCPV-17 and CrCPV-17 isolates from the mosquitoes Uranotaenia sapphirina and Culex restuans, respectively. The SuCPV electropherotype appears to show significant differences from those of the previously characterized lepidopteran Cypoviruses. Sequence analysis of SuCPV segment 10 shows that it is unrelated to either of the two CPV isolates from Diptera or to the CPV species for which Seg-10 has been previously characterized from Lepidoptera. A comparison of the terminal regions of SuCPV genome segments to those of CPV-1, 2, 4, 5 14, 15, 16, 17, 18, and 19 also revealed only low levels of conservation. We therefore, propose that SuCPV is classified within a new Cypovirus species, which we have tentatively identified as Cypovirus-20. We have therefore referred to this virus isolate as S. ubiquitum CPV-20 (SuCPV-20).
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molecular and biological characterization of a Cypovirus from the mosquito culex restuans
Journal of Invertebrate Pathology, 2006Co-Authors: Terry B Green, G. R. Carner, Peter P. C. Mertens, Alexandra M Shapiro, Susan E White, James J BecnelAbstract:A Cypovirus from the mosquito Culex restuans (named CrCPV) was isolated and its biology, morphology, and molecular characteristics were investigated. CrCPV is characterized by small (0.1–1.0m), irregularly shaped inclusion bodies that are multiply embedded. Laboratory studies demonstrated that divalent cations inXuenced transmission of CrCPV to Culex quinquefasciatus larvae; magnesium enhanced CrCPV transmission by »30% while calcium inhibited transmission. CrCPV is the second Cypovirus from a mosquito that has been conWrmed by using molecular analysis. CrCPV has a genome composed of 10 dsRNA segments with an electropherotype similar to the recently discovered UsCPV-17 from the mosquito Uranotaenia sapphirina, but distinct from the lepidopteran Cypoviruses BmCPV-1 (Bombyx mori) and TnCPV-15 (Trichoplusia ni). Nucleotide and deduced amino acid sequence analysis of CrCPV segment 10 (polyhedrin) suggests that CrCPV is closely related (83% nucleotide sequence identity and 87% amino acid sequence identity) to the newly characterized UsCPV-17 but is unrelated to the 16 remaining CPV species from lepidopteran hosts. A comparison of the terminal segment regions of CrCPV and UsCPV-17, an additional method for diVerentiating various Cypovirus species, revealed a high level of conservation. Therefore, we propose that CrCPV is a member of the Cypovirus-17 group and designate this species as CrCPV-17.
Kyoji Hagiwara - One of the best experts on this subject based on the ideXlab platform.
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Nucleotide sequences of segments 1, 3 and 4 of the genome of Bombyx mori Cypovirus 1 encoding putative capsid proteins VP1, VP3 and VP4, respectively.
The Journal of general virology, 2020Co-Authors: Kyoji Hagiwara, Simon W Scott, Gerald R CarnerAbstract:The complete nucleotide sequences of genomic segments S1, S3 and S4 from Bombyx mori Cypovirus 1 (BmCPV-1) have been determined. The segments consisted of 4190, 3846 and 3262 nucleotides encoding putative proteins of 1333, 1239 and 1058 amino acids with molecular masses of approximately 148, 140 and 120 kDa (p148, p140 and p120, respectively). All segments possess a single open reading frame. Homology searches showed that all three proteins have homologies to proteins of Rice ragged stunt virus, a member of the genus Oryzavirus within the family REOVIRIDAE: Partial homologies of p140 to structural proteins in other viruses were also found. The predicted molecular masses and the homologies with structural proteins in other viruses lead us to suggest that S1, S3 and S4 encode the capsid proteins VP1, VP3, and VP4, respectively, of BmCPV-1.
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assembly into single shelled virus like particles by major capsid protein vp1 encoded by genome segment s1 of bombyx mori Cypovirus 1
Journal of General Virology, 2003Co-Authors: Kyoji Hagiwara, Hisashi NaitowAbstract:The major capsid protein VP1 encoded by genome segment S1 of Bombyx mori Cypovirus 1 was expressed in a baculovirus system. In the absence of any other capsid proteins, VP1 was found to assemble into single-shelled virus-like particles. The VP1 particles were more sensitive to acidic conditions than were intact particles.
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nucleotide sequences of segments 1 3 and 4 of the genome of bombyx mori Cypovirus 1 encoding putative capsid proteins vp1 vp3 and vp4 respectively
Journal of General Virology, 2002Co-Authors: Kyoji Hagiwara, S. W. Scott, G. R. CarnerAbstract:The complete nucleotide sequences of genomic segments S1, S3 and S4 from Bombyx mori Cypovirus 1 (BmCPV-1) have been determined. The segments consisted of 4190, 3846 and 3262 nucleotides encoding putative proteins of 1333, 1239 and 1058 amino acids with molecular masses of approximately 148, 140 and 120 kDa (p148, p140 and p120, respectively). All segments possess a single open reading frame. Homology searches showed that all three proteins have homologies to proteins of Rice ragged stunt virus, a member of the genus Oryzavirus within the family Reoviridae. Partial homologies of p140 to structural proteins in other viruses were also found. The predicted molecular masses and the homologies with structural proteins in other viruses lead us to suggest that S1, S3 and S4 encode the capsid proteins VP1, VP3, and VP4, respectively, of BmCPV-1.
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nucleotide sequences of genome segments 6 and 7 of bombyx mori Cypovirus 1 encoding the viral structural proteins v4 and v5 respectively
Journal of General Virology, 2000Co-Authors: Kyoji Hagiwara, Tsuguo MatsumotoAbstract:Nucleotide sequence analyses of cDNAs derived from the double-stranded RNA genome segments 6 and 7 (S6 and S7) of Bombyx mori Cypovirus 1 (BmCPV-1) have revealed that they consist of 1796 and 1501 nucleotides encoding putative proteins of 561 and 448 amino acids with molecular masses of 63604 and 49875 (p64 and p50), respectively. The amino acid sequence of p64, which has a high leucine residue content (10%), contains a leucine zipper motif. Antiserum raised against p64 specifically bound to a viral structural protein of ca. 68 kDa (V4), while antiserum against p50, which specifically bound to a protein of ca. 56 kDa in BmN4 cells infected with BmCPV-1, reacted with a cluster of four viral structural proteins ranging from ca. 34 to 40 kDa (V5). These observations indicate that p50 might be cleaved to V5 during the formation of virus particles.
