Functional characterization of Bombyx mori nucleopolyhedrovirus CG30 protein

Ishihara, Genki; Shimada, Toru; Katsuma, Susumu

doi:10.1016/j.virusres.2013.02.014

Cited by 16 publications

(10 citation statements)

References 21 publications

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“…Autographa californica MNPV (AcMNPV) lacking cg30 was found to replicate in a similar fashion as wild-type virus in cell culture or in insects (Passarelli and Miller, 1994). A cg30 knockout mutant of Bombyx mori NPV, however, produced fewer budded virions (BVs) and OBs and took 24 h longer than wild-type BmNPV to kill infected insects (Ishihara et al, 2013). Speed of kill was not affected in case of vSeBacAL1D76, in contrast to the observations of Ishihara et al (2013), perhaps due to the different virus-host systems employed.…”

Section: Discussionmentioning

confidence: 93%

“…Furthermore, a SNP mutation was detected at position 75,006 in the RING finger of cg30 (se76). SE76 encodes for a protein of 468 amino acids with two functional motifs, a RING finger and a leucine zipper (Ishihara et al, 2013;Passarelli and Miller, 1994). Mutants lacking cg30 in Bombyx mori NPV produced fewer budded viruses and released lower number of occlusion bodies into the hemolymph of infected larvae, and reduced the speed of kill (Ishihara et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

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Identification of Spodoptera exigua nucleopolyhedrovirus genes involved in pathogenicity and virulence

Serrano

Pijlman

Vlak

et al. 2015

Journal of Invertebrate Pathology

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Section: Discussionmentioning

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Identification of Spodoptera exigua nucleopolyhedrovirus genes involved in pathogenicity and virulence

Serrano

Pijlman

Vlak

et al. 2015

Journal of Invertebrate Pathology

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“…BmCG30D-1 is a BmNPV mutant in which cg30, the gene located adjacent to the vp39 gene (Fig. 2), was disrupted by insertion of a lacZ gene cassette (32). VP39-mut produced fewer OBs than VP39-wt in BmN-4 cells (Fig.…”

Section: Figmentioning

confidence: 99%

A Conserved Glycine Residue Is Required for Proper Functioning of a Baculovirus VP39 Protein

Katsuma

Kokusho

2017

J Virol

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The baculovirus VP39 protein is a major nucleocapsid protein essential for viral propagation. However, the critical domains or residues of the VP39 protein have not yet been identified. Here, we performed mutagenesis experiments with Bombyx mori nucleopolyhedrovirus (BmNPV) using 5-bromo-2=-deoxyuridine and isolated a BmNPV mutant that produced fewer occlusion bodies than the wild-type virus. This mutant also produced fewer infectious budded viruses (BVs) than the wildtype virus in both cultured cells and B. mori larvae. Marker rescue experiments using genomic libraries identified a single nucleotide mutation in the vp39 gene. This mutation resulted in an amino acid substitution at glycine 276 (Gly-276) to serine, which was required for all the defective phenotypes observed in the mutant. Sequence comparison revealed that this residue is completely conserved among the VP39 proteins of the sequenced alphabaculoviruses, betabaculoviruses, and gammabaculoviruses. Although early viral gene expression was not significantly affected, the level of expression of a late gene, vcath, was reduced. In addition, two of the very late genes were markedly downregulated in cells infected with this mutant. Western blot and quantitative PCR analyses revealed that the BVs produced from cells infected with this mutant contained smaller amounts of the VP39 protein and viral genomic DNA than those produced from wild-type virus-infected cells. Combined with the results of transmission electron microscopy, VP39 Gly-276 can be concluded to be essential for correct nucleocapsid assembly, viral DNA packaging, and viral gene expression, especially of very late genes. IMPORTANCEThe major nucleocapsid protein gene vp39 is one of the most wellknown baculovirus genes. Although several viral and host proteins that interact with the VP39 protein have been identified, the functionally important domains or residues of this protein remain unknown. The present study revealed that the glycine residue at residue 276, which is completely conserved among sequenced alphabaculoviruses, betabaculoviruses, and gammabaculoviruses, is important for the VP39 function, i.e., structural assembly of nucleocapsids and viral DNA packaging. Moreover, our results provide evidence for the link between nucleocapsid formation and the transcription of viral very late genes.KEYWORDS baculovirus, nucleocapsid, BmNPV, VP39, few polyhedra T he Baculoviridae are a large family of viruses that infect insects, particularly those of the order Lepidoptera. Baculoviruses have a large circular, supercoiled, and doublestranded DNA genome packaged into rod-shaped virions (1, 2). They are divided into four genera, i.e., Alphabaculovirus, Betabaculovirus, Gammabaculovirus, and Deltabaculovirus (3). On the basis of molecular phylogenetic studies using genome sequences, alphabaculoviruses can be further subdivided into group I and II nucleopolyhedroviruses (NPVs) (4). NPVs produce two types of virions during their infection cycle.

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“…BmN-4 cells (2.5 ϫ 10 5 cells per 35-mm diameter dish) were transfected with plasmid DNAs (2 g) using FuGENE HD. Three days after transfection, the localization of Masc-EGFP fusion proteins was examined using a FLoid TM cell imaging station (Life Technologies) (19). The splicing patterns of Bmdsx and BmIMP expression were examined as described above.…”

Section: Localization Of Egfp-fused Mascmentioning

confidence: 99%

Two Conserved Cysteine Residues Are Required for the Masculinizing Activity of the Silkworm Masc Protein

Katsuma

Sugano

Kiuchi

et al. 2015

Journal of Biological Chemistry

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Background:The functional domains of the silkworm masculinizing protein Masc are unknown. Results: The essential region and residues involved in the masculinizing activity of the Masc protein are identified. Conclusion: Masc functions as the masculinizing protein via its C-terminal region but not two zinc finger domains in the N-terminal region. Significance: Our study suggests the mode of action of the masculinizing protein.

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Functional characterization of Bombyx mori nucleopolyhedrovirus CG30 protein

Cited by 16 publications

References 21 publications

Identification of Spodoptera exigua nucleopolyhedrovirus genes involved in pathogenicity and virulence

Identification of Spodoptera exigua nucleopolyhedrovirus genes involved in pathogenicity and virulence

A Conserved Glycine Residue Is Required for Proper Functioning of a Baculovirus VP39 Protein

Two Conserved Cysteine Residues Are Required for the Masculinizing Activity of the Silkworm Masc Protein

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