Networks of protein-protein interactions among structural proteins of budded virus of Bombyx mori nucleopolyhedrovirus

Bombyx mori nucleopolyhedrovirus (BmNPV) BmP95 is a highly conserved gene that is found in all of the baculovirus genomes sequenced to date and is also found in nudiviruses. To investigate the role of BmP95 in virus infection in vitro, a BmP95 deletion virus (vBmP95-De) was generated by homologous recombination in Escherichia coli. Fluorescence and light microscopy and titration analysis indicated that the BmP95 deletion bacmid led to a defect in production of infectious budded virus (BV). However, deletion of BmP95 did not affect viral DNA replication. Electron microscopy showed that masses of aberrant tubular structures were present in cells transfected with the BmP95 deletion bacmid, indicating that deletion of BmP95 affected assembly of the nucleocapsid. This defect could be rescued by insertion of full-length BmP95 into the polyhedrin locus of the BmP95-knockout bacmid but not the N-terminal domain of BmP95. Together, these results showed that full-length BmP95 is essential for BV production and is required for nucleocapsid assembly.

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Disruption of Bombyx mori nucleopolyhedrovirus ORF71 (Bm71) results in inefficient budded virus production and decreased virulence in host larvae

Virus Genes ◽

10.1007/s11262-012-0757-2 ◽

2012 ◽

Vol 45 (1) ◽

pp. 161-168 ◽

Cited By ~ 6

Author(s):

Min-Juan Zhang ◽

Ruo-Lin Cheng ◽

Yi-Han Lou ◽

Wan-Lu Ye ◽

Tao Zhang ◽

...

Keyword(s):

Bombyx Mori ◽

Virus Production ◽

Bombyx Mori Nucleopolyhedrovirus ◽

Budded Virus

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Insilico identification of protein-protein interactions in Silkworm, Bombyx mori

Bioinformation ◽

10.6026/97320630010056 ◽

2014 ◽

Vol 10 (2) ◽

pp. 56-62 ◽

Cited By ~ 3

Author(s):

Ramasamy Sumathy ◽

◽

Ashwath Rao ◽

Nalavadi Chandrakanth ◽

Velliyur Gopalakrishnan

Keyword(s):

Bombyx Mori ◽

Protein Interactions ◽

Protein Protein Interactions ◽

Silkworm Bombyx Mori

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The nematode homologue of Mediator complex subunit 28, F28F8.5, is a critical regulator of C. elegans development

10.7287/peerj.preprints.2530v2 ◽

2016 ◽

Author(s):

Markéta Kostrouchová ◽

David Kostrouch ◽

Ahmed A Chughtai ◽

Filip Kaššák ◽

Jan P. Novotný ◽

...

Keyword(s):

Rna Polymerase Ii ◽

Protein Interactions ◽

Structural Proteins ◽

Mediator Complex ◽

Cytoplasmic Localization ◽

Protein Protein Interactions ◽

C Elegans ◽

Evolutionarily Conserved ◽

Nuclear Events ◽

Bona Fide

The evolutionarily conserved Mediator complex is a critical player in regulating transcription. Comprised of approximately two dozen proteins, Mediator integrates diverse regulatory signals through direct protein-protein interactions that, in turn, modulate the influence of Mediator on RNA Polymerase II activity. One Mediator subunit, MED28, is known to interact with cytoplasmic structural proteins, providing a potential direct link between cytoplasmic dynamics and the control of gene transcription. Although identified in many animals and plants, MED28 is not present in yeast; no bona fide MED28 has been described previously in C. elegans. Here, we identify bioinformatically F28F8.5, an uncharacterized predicted protein, as the nematode homologue of MED28. As in other metazoa, F28F8.5 has dual nuclear and cytoplasmic localization and plays critical roles in the regulation of development. F28F8.5 is a vital gene and its null mutants have severely malformed gonads and do not reproduce. Our results indicate that F28F8.5 is a homologue of MED28 and suggest that the potential to link cytoplasmic and nuclear events is conserved between MED28 vertebrate and nematode homologues.

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Bombyx mori Nucleopolyhedrovirus p26 Is Associated with Viral Late Stage Replication

Insects ◽

10.3390/insects12080707 ◽

2021 ◽

Vol 12 (8) ◽

pp. 707

Author(s):

Jun-Qing Ge ◽

Zhu-Hong Wang ◽

Xi Chen ◽

Hua Chen ◽

Jian Huang

Keyword(s):

Infected Cell ◽

Bombyx Mori ◽

Infectious Virus ◽

Pcr Analysis ◽

Immunofluorescence Analysis ◽

Bombyx Mori Nucleopolyhedrovirus ◽

Cell Cytoplasm ◽

Infected Cells ◽

Budded Virus ◽

Infection Stage

Bombyx mori nucleopolyhedrovirus (BmNPV) p26 is conserved among all Lepidoptera baculoviruses that have been completely sequenced thus far, and some baculoviruses even have two copies of p26, which suggested that p26 may play an important role in the virus infection cycle. This study aimed to characterize BmNPV p26. We found that BmNPV p26 transcripts were detectable as early as 3 h post-infection (hpi), and the transcript levels rapidly increased starting from 12 hpi. Western blot analysis using an anti-p26 polyclonal antibody demonstrated that the corresponding protein was also detectable from 6 hpi in BmNPV-infected cell lysates. Immunofluorescence analysis demonstrated that p26 was mainly dispersed in the infected cell cytoplasm, whereas the over-expressed fusion protein EGFP-p26 also accumulated in the nucleus. These results indicated that p26 is an early BmNPV gene and has functions both in the cytoplasm and the nucleus. RNAi-based knockdown of p26 could produce infectious virus and normal-appearing virions but decreased budded virus (BV) production in BmNPV-infected cells at 72 hpi. Moreover, the results of further quantitative PCR (Q-PCR) analysis indicated that the gp64 and p74 transcripts levels decreased significantly. These results indicated that BmNPV p26 may be associated with BmNPV replication during the late infection stage.

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Efficient Incorporation of Tegument Proteins pUL46, pUL49, and pUS3 into Pseudorabies Virus Particles Depends on the Presence of pUL21

Journal of Virology ◽

10.1128/jvi.01801-06 ◽

2006 ◽

Vol 81 (2) ◽

pp. 1048-1051 ◽

Cited By ~ 22

Author(s):

Kathrin Michael ◽

Barbara G. Klupp ◽

Axel Karger ◽

Thomas C. Mettenleiter

Keyword(s):

Virus Particle ◽

Protein Interactions ◽

Pseudorabies Virus ◽

Structural Proteins ◽

Tegument Protein ◽

Wild Type ◽

Protein Protein Interactions ◽

Virus Particles ◽

Tegument Proteins ◽

Drastic Decrease

ABSTRACT The mature virion of the alphaherpesvirus pseudorabies virus (PrV) contains a minimum of 31 structural proteins which are recruited into the virus particle by a network of protein-protein interactions which is only incompletely understood. We show here that deletion of the tegument protein pUL21 resulted in a drastic decrease in the incorporation of the pUL46, pUL49, and pUS3 tegument components into mature virions. Moreover, the attenuated PrV strain Bartha (PrV-Ba), which, among other defects, carries mutations in pUL21, also fails to package pUL46, pUL49, and pUS3 efficiently. By the reconstitution of wild-type pUL21 expression to PrV-Ba and the transfer of mutated PrV-Ba pUL21 into wild-type PrV, we demonstrate that this phenotype is due to the mutated pUL21.

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Bombyx mori nucleopolyhedrovirus F-like protein Bm14 is a cofactor for GP64-Mediated efficient infection via forming a complex on the envelope of budded virus

Virology ◽

10.1016/j.virol.2019.10.008 ◽

2020 ◽

Vol 539 ◽

pp. 61-68 ◽

Cited By ~ 3

Author(s):

Weifan Xu ◽

Haiping Wang ◽

Hang Liu ◽

Xiaofeng Wu

Keyword(s):

Bombyx Mori ◽

Bombyx Mori Nucleopolyhedrovirus ◽

Budded Virus

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Linkage map of protein–protein interactions of Porcine teschovirus

Journal of General Virology ◽

10.1099/vir.0.81144-0 ◽

2005 ◽

Vol 86 (10) ◽

pp. 2763-2768 ◽

Cited By ~ 10

Author(s):

Roland Zell ◽

Simone Seitz ◽

Andreas Henke ◽

Thomas Munder ◽

Peter Wutzler

Keyword(s):

Linkage Map ◽

Protein Interactions ◽

Structural Proteins ◽

Protein Protein Interactions ◽

Yeast Two Hybrid ◽

Protein L ◽

Leader Protein ◽

Porcine Teschovirus ◽

Two Hybrid

A yeast two-hybrid study was conducted to catalogue the protein–protein interactions of the Porcine teschovirus non-structural proteins. Five homodimer, three reciprocal heterodimer and four unidirectional heterodimer interactions were observed. While several interactions are similar to those described in previous studies using enteroviruses, such as homo- and heterodimeric interactions of the 2B, 3CD and 3D proteins, several were not found previously. Among these is the binding of the leader protein L to the proteinases 3C and 3CD. Unlike the poliovirus 3C, the teschovirus 3C proteinase dimerizes and interacts with 2BC, 3CD and 3D. The strongest interactions were observed for L–3C, L–3CD and 3C–3CD.

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