Baculoviridae

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Hualin Wang - One of the best experts on this subject based on the ideXlab platform.

  • Functional Characterization of the Group I Alphabaculovirus Specific Gene ac73
    Virologica Sinica, 2019
    Co-Authors: Wei Shao, Lihong He, Qingxiu Chen, Zhihong Hu, Hualin Wang, Fei Deng, Jiang Li, Manli Wang
    Abstract:

    Baculoviridae is a family of large DNA viruses that specifically infect insects. It contains four genera, Alpha-, Beta-, Gamma-, and Deltabaculovirus. Alphabaculovirus is further divided into Group I and II, and Group I appears to be emerged most recently among all baculoviruses. Interestingly, there are 12 Group I specific genes that are only found in this lineage. Studying these genes is helpful to understand how baculoviruses evolved. Here, we reported the functional analyzing results of ac73, a function unknown Group I specific gene of Autographa californica multiple nucleopolyhedrovirus (AcMNPV) which is the type species of baculovirus. The AC73 protein encoded by ac73 was found to be expressed during the late stage of infection and incorporated into the nucleocapsids of budded virus (BV) and occlusion-derived virus (ODV). In infected cells, AC73 resided mainly in the ring zone region of the nucleus, and appeared to be assembled into occlusion bodies (OBs). The ac73 knockout and repaired viruses were constructed and studied by in vitro and in vivo infection. Although ac73 was not essential for BV and ODV or OB formation, the BV titer and viral infectivity in insect larvae of ac73 knockout AcMNPV decreased by about 5–8 and 3–4 fold compared to those of wild type virus, respectively, suggesting ac73 contributed to infectious BV production and viral infectivity in vivo. This research provides new insight into the function of this Group I specific gene.

  • Deltabaculoviruses encode a functional type I budded virus envelope fusion protein.
    The Journal of general virology, 2017
    Co-Authors: Manli Wang, Hualin Wang, Shu Shen, James J. Becnel
    Abstract:

    Envelope fusion proteins (F proteins) are major constituents of budded viruses (BVs) of alpha- and betabaculoviruses (Baculoviridae) and are essential for the systemic infection of insect larvae and insect cell culture. An f homologue gene is absent in gammabaculoviruses. Here we characterized the putative F-homologue (Cuni-F), encoded by (ORF) 104 of Culex nigripalpus nucleopolyhedrovirus (CuniNPV), the only deltabaculovirus member. When expressed alone, this protein seems to locate on the cell surface and is able to induce cell–cell fusion. When expressed by an alphabaculovirus (Autographa california nucleopolyhedrovirus), it was found to be incorporated into BVs. Western blot analyses detected the uncleaved Cuni-F0 and the furin-cleaved F1 forms. Treatment of infected cells with tunicamycin showed that Cuni-F contains N-glycans. Mutagenesis analysis identified the canonical furin cleavage site 126RARR129 as being responsible for the cleavage of Cuni-F in insect cells. The collective evidence suggests that CuniNPV encodes a functional F protein.

  • partial functional rescue of helicoverpa armigera single nucleocapsid nucleopolyhedrovirus infectivity by replacement of f protein with gp64 from autographa californica multicapsid nucleopolyhedrovirus
    Journal of Virology, 2010
    Co-Authors: Manli Wang, Fei Deng, Just M. Vlak, Shu Shen, Feifei Yin, Ying Tan, Hualin Wang
    Abstract:

    Two distinct envelope fusion proteins (EFPs) (GP64 and F) have been identified in members of the Baculoviridae family of viruses. F proteins are found in group II nucleopolyhedroviruses (NPVs) of alphabaculoviruses and in beta- and deltabaculoviruses, while GP64 occurs only in group I NPVs of alphabaculoviruses. It was proposed that an ancestral baculovirus acquired the gp64 gene that conferred a selective advantage and allowed it to evolve into group I NPVs. The F protein is a functional analogue of GP64, as evidenced from the rescue of gp64-null Autographa californica multicapsid nucleopolyhedrovirus (MNPV) (AcMNPV) by F proteins from group II NPVs or from betabaculoviruses. However, GP64 failed to rescue an F-null Spodoptera exigua MNPV (SeMNPV) (group II NPV). Here, we report the successful generation of an infectious gp64-rescued group II NPV of Helicoverpa armigera (vHaBacΔF-gp64). Viral growth curve assays and quantitative real-time PCR (Q-PCR), however, showed substantially decreased infectivity of vHaBacΔF-gp64 compared to the HaF rescue control virus vHaBacΔF-HaF. Electron microscopy further showed that most vHaBacΔF-gp64 budded viruses (BV) in the cell culture supernatant lacked envelope components and contained morphologically aberrant nucleocapsids, suggesting the improper BV envelopment or budding of vHaBacΔF-gp64. Bioassays using pseudotyped viruses with a reintroduced polyhedrin gene showed that GP64-pseudotyped Helicoverpa armigera single nucleocapsid nucleopolyhedrovirus (HearNPV) significantly delayed the mortality of infected H. armigera larvae.

  • identification of protein protein interactions of the occlusion derived virus associated proteins of helicoverpa armigera nucleopolyhedrovirus
    Journal of General Virology, 2010
    Co-Authors: Ke Peng, Fei Deng, Jingjiao Song, Chunsheng Dong, Hualin Wang
    Abstract:

    The purpose of this study was to identify protein–protein interactions among the components of the occlusion-derived virus (ODV) of Helicoverpa armigera nucleopolyhedrovirus (HearNPV), a group II alphabaculovirus in the family Baculoviridae. To achieve this, 39 selected genes of potential ODV structural proteins were cloned and expressed in the Gal4 yeast two-hybrid (Y2H) system. The direct-cross Y2H assays identified 22 interactions comprising 13 binary interactions [HA9–ODV-EC43, ODV-E56–38K, ODV-E56–PIF3, LEF3–helicase, LEF3–alkaline nuclease (AN), GP41–38K, GP41–HA90, 38K–PIF3, 38K–PIF2, VP80–HA100, ODV-E66–PIF3, ODV-E66–PIF2 and PIF3–PIF2] and nine self-associations (IE1, HA44, LEF3, HA66, GP41, CG30, 38K, PIF3 and P24). Five of these interactions – LEF3–helicase and LEF3–AN, and the self-associations of IE1, LEF3 and 38K – have been reported previously in Autographa californica multiple nucleopolyhedrovirus. As HA44 and HA100 were two newly identified ODV proteins of group II viruses, their interactions were further confirmed. The self-association of HA44 was verified with a His pull-down assay and the interaction of VP80–HA100 was confirmed by a co-immunoprecipitation assay. A summary of the protein–protein interactions of baculoviruses reported so far, comprising 68 interactions with 45 viral proteins and five host proteins, is presented, which will facilitate our understanding of the molecular mechanisms of baculovirus infection.

  • Partial Functional Rescue of Helicoverpa armigera Single Nucleocapsid Nucleopolyhedrovirus Infectivity by Replacement of F Protein
    2010
    Co-Authors: Gp From Autographa Californica, Multicapsid Nucleopolyhedrovirus, Hualin Wang
    Abstract:

    Two distinct envelope fusion proteins (EFPs) (GP64 and F) have been identified in members of the Baculoviridae family of viruses. F proteins are found in group II nucleopolyhedroviruses (NPVs) of alphabaculoviruses and in beta- and deltabaculoviruses, while GP64 occurs only in group I NPVs of alphabaculoviruses. It was proposed that an ancestral baculovirus acquired the gp64 gene that conferred a selective advantage and allowed it to evolve into group I NPVs. The F protein is a functional analogue of GP64, as evidenced from the rescue of gp64-null Autographa californica multicapsid nucleopolyhedrovirus (MNPV) (AcMNPV) by F proteins from group II NPVs or from betabaculoviruses. However, GP64 failed to rescue an F-null Spodoptera exiguaMNPV (SeMNPV) (group II NPV). Here, we report the successful generation of an infectious gp64-rescued group II NPV of Helicoverpa armigera (vHaBacF-gp64). Viral growth curve assays and quantitative real-time PCR (Q-PCR), however, showed substan-tially decreased infectivity of vHaBacF-gp64 compared to the HaF rescue control virus vHaBacF-HaF. Electron microscopy further showed that most vHaBacF-gp64 budded viruses (BV) in the cell culture supernatant lacked envelope components and contained morphologically aberrant nucleocapsids, suggesting the improper BV envel-opment or budding of vHaBacF-gp64. Bioassays using pseudotyped viruses with a reintroduced polyhedrin gene showed that GP64-pseudotyped Helicoverpa armigera single nucleocapsid nucleopolyhedrovirus (HearNPV) signif-icantly delayed the mortality of infected H. armigera larvae

Manli Wang - One of the best experts on this subject based on the ideXlab platform.

  • Functional Characterization of the Group I Alphabaculovirus Specific Gene ac73
    Virologica Sinica, 2019
    Co-Authors: Wei Shao, Lihong He, Qingxiu Chen, Zhihong Hu, Hualin Wang, Fei Deng, Jiang Li, Manli Wang
    Abstract:

    Baculoviridae is a family of large DNA viruses that specifically infect insects. It contains four genera, Alpha-, Beta-, Gamma-, and Deltabaculovirus. Alphabaculovirus is further divided into Group I and II, and Group I appears to be emerged most recently among all baculoviruses. Interestingly, there are 12 Group I specific genes that are only found in this lineage. Studying these genes is helpful to understand how baculoviruses evolved. Here, we reported the functional analyzing results of ac73, a function unknown Group I specific gene of Autographa californica multiple nucleopolyhedrovirus (AcMNPV) which is the type species of baculovirus. The AC73 protein encoded by ac73 was found to be expressed during the late stage of infection and incorporated into the nucleocapsids of budded virus (BV) and occlusion-derived virus (ODV). In infected cells, AC73 resided mainly in the ring zone region of the nucleus, and appeared to be assembled into occlusion bodies (OBs). The ac73 knockout and repaired viruses were constructed and studied by in vitro and in vivo infection. Although ac73 was not essential for BV and ODV or OB formation, the BV titer and viral infectivity in insect larvae of ac73 knockout AcMNPV decreased by about 5–8 and 3–4 fold compared to those of wild type virus, respectively, suggesting ac73 contributed to infectious BV production and viral infectivity in vivo. This research provides new insight into the function of this Group I specific gene.

  • Deltabaculoviruses encode a functional type I budded virus envelope fusion protein.
    The Journal of general virology, 2017
    Co-Authors: Manli Wang, Hualin Wang, Shu Shen, James J. Becnel
    Abstract:

    Envelope fusion proteins (F proteins) are major constituents of budded viruses (BVs) of alpha- and betabaculoviruses (Baculoviridae) and are essential for the systemic infection of insect larvae and insect cell culture. An f homologue gene is absent in gammabaculoviruses. Here we characterized the putative F-homologue (Cuni-F), encoded by (ORF) 104 of Culex nigripalpus nucleopolyhedrovirus (CuniNPV), the only deltabaculovirus member. When expressed alone, this protein seems to locate on the cell surface and is able to induce cell–cell fusion. When expressed by an alphabaculovirus (Autographa california nucleopolyhedrovirus), it was found to be incorporated into BVs. Western blot analyses detected the uncleaved Cuni-F0 and the furin-cleaved F1 forms. Treatment of infected cells with tunicamycin showed that Cuni-F contains N-glycans. Mutagenesis analysis identified the canonical furin cleavage site 126RARR129 as being responsible for the cleavage of Cuni-F in insect cells. The collective evidence suggests that CuniNPV encodes a functional F protein.

  • partial functional rescue of helicoverpa armigera single nucleocapsid nucleopolyhedrovirus infectivity by replacement of f protein with gp64 from autographa californica multicapsid nucleopolyhedrovirus
    Journal of Virology, 2010
    Co-Authors: Manli Wang, Fei Deng, Just M. Vlak, Shu Shen, Feifei Yin, Ying Tan, Hualin Wang
    Abstract:

    Two distinct envelope fusion proteins (EFPs) (GP64 and F) have been identified in members of the Baculoviridae family of viruses. F proteins are found in group II nucleopolyhedroviruses (NPVs) of alphabaculoviruses and in beta- and deltabaculoviruses, while GP64 occurs only in group I NPVs of alphabaculoviruses. It was proposed that an ancestral baculovirus acquired the gp64 gene that conferred a selective advantage and allowed it to evolve into group I NPVs. The F protein is a functional analogue of GP64, as evidenced from the rescue of gp64-null Autographa californica multicapsid nucleopolyhedrovirus (MNPV) (AcMNPV) by F proteins from group II NPVs or from betabaculoviruses. However, GP64 failed to rescue an F-null Spodoptera exigua MNPV (SeMNPV) (group II NPV). Here, we report the successful generation of an infectious gp64-rescued group II NPV of Helicoverpa armigera (vHaBacΔF-gp64). Viral growth curve assays and quantitative real-time PCR (Q-PCR), however, showed substantially decreased infectivity of vHaBacΔF-gp64 compared to the HaF rescue control virus vHaBacΔF-HaF. Electron microscopy further showed that most vHaBacΔF-gp64 budded viruses (BV) in the cell culture supernatant lacked envelope components and contained morphologically aberrant nucleocapsids, suggesting the improper BV envelopment or budding of vHaBacΔF-gp64. Bioassays using pseudotyped viruses with a reintroduced polyhedrin gene showed that GP64-pseudotyped Helicoverpa armigera single nucleocapsid nucleopolyhedrovirus (HearNPV) significantly delayed the mortality of infected H. armigera larvae.

  • the f like protein ac23 enhances the infectivity of the budded virus of gp64 null autographa californica multinucleocapsid nucleopolyhedrovirus pseudotyped with baculovirus envelope fusion protein f
    Journal of Virology, 2008
    Co-Authors: Manli Wang, Fei Deng, Just M. Vlak, Feifei Yin, Ying Tan, Hualin Wang
    Abstract:

    The GP64 and F proteins were previously identified as the sole functional envelope fusion proteins in Baculoviridae. F-like proteins, present only in group I nucleopolyhedroviruses (NPVs), are remnant, nonfunctional F proteins. In this report, we describe the effect of the presence or absence of the F-like protein Ac23 in a gp64-null Autographa californica multinucleocapsid NPV pseudotyped with the F protein from Spodoptera exigua multicapsid NPV (SeF). We found that the presence of Ac23 elevates the infectivity of the pseudotyped virus. This is in contrast to the results of Lung et al. (J. Virol. 76:5729-5736, 2002), who found no such effect. The possible reasons for the differing results are discussed.

George F Rohrmann - One of the best experts on this subject based on the ideXlab platform.

  • Review article Replication of baculovirus DNA
    2013
    Co-Authors: Marcel Kool, Just M. Vlak, Lt Christian H. Ahrens, George F Rohrmann
    Abstract:

    The Baculoviridae is a diverse family of pathogens that are infectious for arthropods and are characterized by a complex replication cycle that culminates in th

  • transfer incorporation and substitution of envelope fusion proteins among members of the Baculoviridae orthomyxoviridae and metaviridae insect retrovirus families
    Journal of Virology, 2002
    Co-Authors: Margot N Pearson, George F Rohrmann
    Abstract:

    Recent research suggests that members of the Baculoviridae family can be divided into two groups on the basis of their envelope fusion proteins (31). One group utilizes proteins related to GP64. Homologs of GP64 are also used by the thogotoviruses (27), a genus of the Orthomyxoviridae family. Members of the other group of baculoviruses utilize envelope fusion proteins related to a protein called LD130. LD130 has been shown to be related to the envelope protein of insect retroviruses in the genus Errantivirus (family Metaviridae) (24, 36). In this review, the evidence for these data is outlined and possible pathways of transfer, incorporation, and substitution are discussed.

  • transfer incorporation and substitution of envelope fusion proteins among members of the Baculoviridae orthomyxoviridae and metaviridae insect retrovirus families
    Journal of Virology, 2002
    Co-Authors: Margot N Pearson, George F Rohrmann
    Abstract:

    Recent research suggests that members of the Baculoviridae family can be divided into two groups on the basis of their envelope fusion proteins (31). One group utilizes proteins related to GP64. Homologs of GP64 are also used by the thogotoviruses (27), a genus of the Orthomyxoviridae family. Members of the other group of baculoviruses utilize envelope fusion proteins related to a protein called LD130. LD130 has been shown to be related to the envelope protein of insect retroviruses in the genus Errantivirus (family Metaviridae) (24, 36). In this review, the evidence for these data is outlined and possible pathways of transfer, incorporation, and substitution are discussed.

  • identification of the lymantria dispar nucleopolyhedrovirus envelope fusion protein provides evidence for a phylogenetic division of the Baculoviridae
    Journal of Virology, 2000
    Co-Authors: Margot N Pearson, Christoph Groten, George F Rohrmann
    Abstract:

    The complete genome sequences of a number of diverse members of the Baculoviridae including both nucleopolyhedroviruses (NPVs) and granuloviruses (GVs) revealed that they lack a homolog of GP64, the envelope fusion protein of the budded form of Autographa californica multinucleocapsid NPV (AcMNPV) and its close relatives. Computer-assisted analyses of the genome of one of these viruses, Lymantria dispar MNPV (LdMNPV), revealed a single open reading frame (ld130) whose product had the predicted properties of a membrane protein. Characterization of the localization of the products of the full-length ld130 gene and of an ld130-enhanced green fluorescent protein gene (egfp) fusion using both immunofluorescence and fluorescence microscopy revealed that LD130 accumulates at the plasma membranes of cells infected with LdMNPV or transfected with ld130-egfp. In addition, cells transfected with either ld130 or ld130-egfp or infected with wild-type virus undergo membrane fusion at pH 5. Western blot analyses indicate that LD130 is present in infected cells as an 83-kDa protein and is also present in budded virions as a protein doublet containing bands of 81 and 83 kDa. Tunicamycin treatment of infected cells resulted in an immunoreactive band of about 72 kDa, indicating that LD130 is N-glycosylated. Whereas the distribution of gp64 appears to be confined to a relatively closely related group of NPVs, homologs of ld130 are present in a diverse number of both NPVs and GVs. This suggests that LD130 may be the primordial baculovirus envelope fusion protein.

Fei Deng - One of the best experts on this subject based on the ideXlab platform.

  • Functional Characterization of the Group I Alphabaculovirus Specific Gene ac73
    Virologica Sinica, 2019
    Co-Authors: Wei Shao, Lihong He, Qingxiu Chen, Zhihong Hu, Hualin Wang, Fei Deng, Jiang Li, Manli Wang
    Abstract:

    Baculoviridae is a family of large DNA viruses that specifically infect insects. It contains four genera, Alpha-, Beta-, Gamma-, and Deltabaculovirus. Alphabaculovirus is further divided into Group I and II, and Group I appears to be emerged most recently among all baculoviruses. Interestingly, there are 12 Group I specific genes that are only found in this lineage. Studying these genes is helpful to understand how baculoviruses evolved. Here, we reported the functional analyzing results of ac73, a function unknown Group I specific gene of Autographa californica multiple nucleopolyhedrovirus (AcMNPV) which is the type species of baculovirus. The AC73 protein encoded by ac73 was found to be expressed during the late stage of infection and incorporated into the nucleocapsids of budded virus (BV) and occlusion-derived virus (ODV). In infected cells, AC73 resided mainly in the ring zone region of the nucleus, and appeared to be assembled into occlusion bodies (OBs). The ac73 knockout and repaired viruses were constructed and studied by in vitro and in vivo infection. Although ac73 was not essential for BV and ODV or OB formation, the BV titer and viral infectivity in insect larvae of ac73 knockout AcMNPV decreased by about 5–8 and 3–4 fold compared to those of wild type virus, respectively, suggesting ac73 contributed to infectious BV production and viral infectivity in vivo. This research provides new insight into the function of this Group I specific gene.

  • partial functional rescue of helicoverpa armigera single nucleocapsid nucleopolyhedrovirus infectivity by replacement of f protein with gp64 from autographa californica multicapsid nucleopolyhedrovirus
    Journal of Virology, 2010
    Co-Authors: Manli Wang, Fei Deng, Just M. Vlak, Shu Shen, Feifei Yin, Ying Tan, Hualin Wang
    Abstract:

    Two distinct envelope fusion proteins (EFPs) (GP64 and F) have been identified in members of the Baculoviridae family of viruses. F proteins are found in group II nucleopolyhedroviruses (NPVs) of alphabaculoviruses and in beta- and deltabaculoviruses, while GP64 occurs only in group I NPVs of alphabaculoviruses. It was proposed that an ancestral baculovirus acquired the gp64 gene that conferred a selective advantage and allowed it to evolve into group I NPVs. The F protein is a functional analogue of GP64, as evidenced from the rescue of gp64-null Autographa californica multicapsid nucleopolyhedrovirus (MNPV) (AcMNPV) by F proteins from group II NPVs or from betabaculoviruses. However, GP64 failed to rescue an F-null Spodoptera exigua MNPV (SeMNPV) (group II NPV). Here, we report the successful generation of an infectious gp64-rescued group II NPV of Helicoverpa armigera (vHaBacΔF-gp64). Viral growth curve assays and quantitative real-time PCR (Q-PCR), however, showed substantially decreased infectivity of vHaBacΔF-gp64 compared to the HaF rescue control virus vHaBacΔF-HaF. Electron microscopy further showed that most vHaBacΔF-gp64 budded viruses (BV) in the cell culture supernatant lacked envelope components and contained morphologically aberrant nucleocapsids, suggesting the improper BV envelopment or budding of vHaBacΔF-gp64. Bioassays using pseudotyped viruses with a reintroduced polyhedrin gene showed that GP64-pseudotyped Helicoverpa armigera single nucleocapsid nucleopolyhedrovirus (HearNPV) significantly delayed the mortality of infected H. armigera larvae.

  • identification of protein protein interactions of the occlusion derived virus associated proteins of helicoverpa armigera nucleopolyhedrovirus
    Journal of General Virology, 2010
    Co-Authors: Ke Peng, Fei Deng, Jingjiao Song, Chunsheng Dong, Hualin Wang
    Abstract:

    The purpose of this study was to identify protein–protein interactions among the components of the occlusion-derived virus (ODV) of Helicoverpa armigera nucleopolyhedrovirus (HearNPV), a group II alphabaculovirus in the family Baculoviridae. To achieve this, 39 selected genes of potential ODV structural proteins were cloned and expressed in the Gal4 yeast two-hybrid (Y2H) system. The direct-cross Y2H assays identified 22 interactions comprising 13 binary interactions [HA9–ODV-EC43, ODV-E56–38K, ODV-E56–PIF3, LEF3–helicase, LEF3–alkaline nuclease (AN), GP41–38K, GP41–HA90, 38K–PIF3, 38K–PIF2, VP80–HA100, ODV-E66–PIF3, ODV-E66–PIF2 and PIF3–PIF2] and nine self-associations (IE1, HA44, LEF3, HA66, GP41, CG30, 38K, PIF3 and P24). Five of these interactions – LEF3–helicase and LEF3–AN, and the self-associations of IE1, LEF3 and 38K – have been reported previously in Autographa californica multiple nucleopolyhedrovirus. As HA44 and HA100 were two newly identified ODV proteins of group II viruses, their interactions were further confirmed. The self-association of HA44 was verified with a His pull-down assay and the interaction of VP80–HA100 was confirmed by a co-immunoprecipitation assay. A summary of the protein–protein interactions of baculoviruses reported so far, comprising 68 interactions with 45 viral proteins and five host proteins, is presented, which will facilitate our understanding of the molecular mechanisms of baculovirus infection.

  • the f like protein ac23 enhances the infectivity of the budded virus of gp64 null autographa californica multinucleocapsid nucleopolyhedrovirus pseudotyped with baculovirus envelope fusion protein f
    Journal of Virology, 2008
    Co-Authors: Manli Wang, Fei Deng, Just M. Vlak, Feifei Yin, Ying Tan, Hualin Wang
    Abstract:

    The GP64 and F proteins were previously identified as the sole functional envelope fusion proteins in Baculoviridae. F-like proteins, present only in group I nucleopolyhedroviruses (NPVs), are remnant, nonfunctional F proteins. In this report, we describe the effect of the presence or absence of the F-like protein Ac23 in a gp64-null Autographa californica multinucleocapsid NPV pseudotyped with the F protein from Spodoptera exigua multicapsid NPV (SeF). We found that the presence of Ac23 elevates the infectivity of the pseudotyped virus. This is in contrast to the results of Lung et al. (J. Virol. 76:5729-5736, 2002), who found no such effect. The possible reasons for the differing results are discussed.

Chuanxi Zhang - One of the best experts on this subject based on the ideXlab platform.

  • The genome of Pieris rapae granulovirus
    2016
    Co-Authors: Baoqin Zhang, Xiaofeng Wang, Ruo-lin Cheng, Chuanxi Zhang
    Abstract:

    Pieris rapae granulovirus (PrGV) can infect and kill larvae of Pieris rapae, a worldwide and important pest of mustard family crops. The PrGV genome consists of 108,592 bp, is AT rich (66.8%), and is most structurally and organizationally similar to the Choristoneura occidentalis granulovirus genome. Of the predicted 120 open reading frames (ORFs), 32 genes specifically oc-curred in GVs, including four genes unique to PrGV (Pr9, Pr32, Pr53, and Pr117). The small cabbage white butterfly (Pieris rapae) is widespreadaround the world and is an important pest of cultivated cab-bages and other mustard family crops. Pieris rapae granulovirus (PrGV) infects and kills larvae of Pieris rapae. PrGV has been widely used for biological control of the small cabbage white but-terfly and has become a commercially important biological insec-ticide. The family Baculoviridae is a diverse group of circular double-strandedDNA viruses.Nucleopolyhedrovirus (NPV) andGranulo-virus (GV) are the two main genera in this family. The GV largely differs from the NPV in the structure of the occlusion bodies. Genome information has greatly expanded our understanding o

  • Genome Sequence of a Bombyx mori Nucleopolyhedrovirus Strain with Cubic Occlusion Bodies
    Journal of virology, 2012
    Co-Authors: Ruo-lin Cheng, Xu Yipeng, Chuanxi Zhang
    Abstract:

    ABSTRACT Bombyx mori nucleopolyhedrovirus (BmNPV) is a typical species of Baculoviridae. The complete genome sequence of a BmNPV strain with cubic occlusion bodies is reported here. The genome of this strain consists of 127,465 nucleotides with a G+C content of 40.36% and is 97.3% and 97.5% identical to those of BmNPV strain T3 and Bombyx mandarina NPV S1, respectively. Despite the abnormal polyhedra it forms, the polyhedrin gene of the BmNPV cubic strain is 100% identical to those of the other two strains. Baculovirus repeated ORFs and homologous repeat regions cause the major differences in genome size of these BmNPV isolates.

  • odv associated proteins of the pieris rapae granulovirus
    Journal of Proteome Research, 2011
    Co-Authors: Xiaofeng Wang, Baoqin Zhang, Haijun Xu, Yipeng Xu, Minjuan Zhang, Chuanxi Zhang
    Abstract:

    Alphabaculovirus (lepidopteran-specific nucleopolyhedroviruses, NPV) and Betabaculovirus (granuloviruses, GV) are two main genera of the family Baculoviridae. The virion proteomes of Alphabaculovir...