THE NATURE OF POLYHEDRIN
Just M. Vlak, George F Rohrmann · Elsevier eBooks · 1985
Cited by 50
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About 768 papers for “Polyhedrin”
Just M. Vlak, George F Rohrmann · Elsevier eBooks · 1985
Cited by 50
Mark A. Gonzalez, Gale Smith, Max D. Summers · Virology · 1989
Cited by 38
Hajime Mori, Hideyuki Nakazawa, Keiko Ikeda · Uirusu · 1998
Cited by 1Open access
Olga V. Konevtsova, Ivan Golushko, Rudolf Podgornik et al. · Nanoscale Advances · 2023
Unlike in other viruses, in Cypoviruses the genome is doubly protected since their icosahedral capsids are embedded into a perfect polyhedrin crystal. Current experimental methods cannot resolve the resulting interface structure and we propose a symmetry-based approach to predict it. We reveal a remarkable match between the surfaces of Cypovirus and the outer polyhedrin matrix. The match arises due to the preservation of the common tetragonal symmetry, allowing perfect contacts of polyhedrin trimers with VP1 and VP5 capsid proteins. We highlight a crucial role of the VP5 proteins in embedding the Cypovirus into the polyhedrin matrix and discuss the relationship between the nucleoside triphosphatase activity of the proteins and their role in the superstructure formation. Additionally, we propose an electrostatic mechanism that drives the viral superstructure disassembly occurring in the alkaline environment of the insect intestines. Our study may underpin novel strategies for engineering proteinaceous nanocontainers in diverse biotechnological and chemical applications.
Cited by 3Open access
Chih‐Ming Chou, Chang-Jen Huang, Chu‐Fang Lo et al. · Journal of Invertebrate Pathology · 1996
Cited by 28
차형준 · Open Access System for Information Sharing (Pohang University of Science and Technology) · 2018
Cited by 0
Guillaume Carissimo (2636878), Karin Eiglmeier (8102), Julie Reveillaud (225126) et al. · Figshare · 2016
<p>(A) Neighbor-joining tree of RNA-dependent RNA polymerase (RdRp) sequences of Cypoviruses, (B) Neighbor-joining tree of polyhedrin sequences of Cypoviruses. Multiple protein alignment was performed with the longest ORF (corresponding to the polymerase) for each nucleic acid. NJ bootstrap values (above 0.75) are indicated above branches. Pairwise distances are indicated in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0153881#pone.0153881.s010" target="_blank">S6 File</a>.</p>
Cited by 0Open access
Mei Yin, Xinyu Tong, Yongjie Feng et al. · International Journal of Biological Macromolecules · 2024
Cited by 3
Shang, Hui · OhioLink ETD Center (Ohio Library and Information Network) · 2018
Cited by 0Open access
NTUR (臺灣機構典藏) · 1996
Cited by 0
Seyed E. Hasnain, Sudip Ghosh, Anjali Jain et al. · 1998
Cited by 0
Yipeng Qi, Zi-Ye Liu, Jiawang Wang et al. · Biodiversity Science · 1997
Cited by 0Open access
Sung Min Bae (401039), Hee Jung Kim (401040), Jun Beom Lee (401041) et al. · Figshare · 2015
<p>Sf21 cells were infected at an MOI of 5 with each virus and harvested at 4 days post-infection. Protein samples were analyzed by SDS-PAGE (A) and Western blot analysis with E2 monoclonal antibody (B).</p>
Cited by 0Open access
Guanping Chen, Shudi Zhao, Nan Chen et al. · Gene · 2021
Cited by 4
Axford, D, Ji, X, Stuart, DI et al. · Oxford University Research Archive (ORA) (University of Oxford) · 2014
This work demonstrates that with the use of a microfocus synchrotron beam the structure of a novel viral polyhedrin could be successfully determined from microcrystals within cells, removing the preparatory step of sample isolation and maintaining a favourable biological environment. The data obtained are of high quality, comparable to that obtained from isolated crystals, and enabled a facile structure determination. A small but significant difference is observed between the unit-cell parameters and the mosaic spread of in cellulo and isolated crystals, suggesting that even these robust crystals are adversely affected by removal from the cell.
Cited by 1Open access
Zhìhóng Hú, MengXin Liu, F. Jin et al. · Journal of General Virology · 1993
A portion of the genome of the Buzura suppressaria (Lepidoptera) single nucleocapsid nuclear polyhedrosis virus (BsSNPV) containing the polyhedrin gene was sequenced. An open reading frame of 738 nucleotides encoded a protein of 246 amino acids and represented the polyhedrin gene. A conserved TAAG motif, associated with transcriptional start sites in other polyhedrin genes, was identified 51 nucleotides upstream of the BsSNPV polyhedrin gene. A putative polyadenylation signal, AATAAA, was found immediately downstream of the polypeptide termination codon. Comparison of the amino acid sequence of BsSNPV polyhedrin with other NPV polyhedrins and granulosis virus granulins showed that the BsSNPV polyhedrin was most closely related to the polyhedrin of Orgyia pseudotsugata (Lepidoptera) SNPV and most distantly related to the polyhedrin of Neodiprion sertifer (Hymenoptera) SNPV.
Cited by 30Open access
차형준 · Open Access System for Information Sharing (Pohang University of Science and Technology) · 2018
Cited by 0
Hiroshi Nakazawa, Frédéric Kendirgi, S. Belloncik et al. · Journal of General Virology · 1996
We have already cloned the polyhedrin genes of the wild-type strain H Bombyx mori cytoplasmic polyhedrosis virus (BmCPV) and its mutant, strain A. In this work, polyhedrin genes of mutant BmCPV strains C1 and C2 were cloned and their nucleotide sequences were determined. The polyhedrin amino acid sequences of strains C1 and C2 were compared with that of strain H. Strains C1 and C2 contained two and three sites of mutation in their polyhedrin genes, respectively. Four amino acids (249RLLV) were added at the carboxy terminus of the polyhedrin of strain A, C1 and C2 and the corresponding polyhedrin genes were introduced into a baculovirus expression vector. Intracellular localization of expressed polyhedrin as well as the morphology and localization of polyhedra were investigated by Western blot and microscopy analysis. Recombinant baculovirus containing the polyhedrin gene of strain H produced hexahedral polyhedra in both the cytoplasm and the nucleus. However, the hexahedral polyhedra of strain A were localized only in the nucleus. Normal polyhedra were not observed in cells infected with recombinant baculoviruses expressing strain C1 or C2 polyhedrin genes, but amorphous structures were found in infected cells. Results of expression of a chimaeric luciferase-containing carboxyl-terminal sequence of strain A demonstrated that this sequence was responsible for the nuclear localization. We suggest that a mutation at the carboxy terminus of BmCPV polyhedrin led to nuclear localization of polyhedrin and that several other mutations were responsible for modification of the crystallization pattern of polyhedrin.
Cited by 9
Zoe Putman · Maryland Shared Open Access Repository (USMAI Consortium) · 2020
While the baculovirus expression vector system (BEVS) has proved its ability to produce high quality recombinant proteins utilizing a eukaryotic host, limited improvements have been made with regards to expressing multiple proteins. Current co-expression protocols utilize native baculovirus promoters which have limited versatility and varying expression levels. This thesis work aims to address these limitations, through the evaluation of modified AcMNPV polyhedrin promoters with the end goal of identifying novel promoters that display varying levels of expression and provide greater control over the ratio of recombinant proteins produced in the cell. Initial promoter screening measured fluorescence output of an eGFP reporter. Promoters of the most interest were then evaluated for test protein expression to determine their ability to produce more complex proteins. Mutations within the minimal promoter region which disrupt critical promoter elements were found to severely impair promoter activity. On the other hand, those which altered the upstream region beyond the transcription start site had little influence on reporter gene levels. Mutations to the polyhedrin promoter CAGT motif which unexpectedly introduced an alternative translation start site (CAtg), appeared to significantly impact downstream gene expression. When this mutation was in-frame with the reporter gene, eGFP expression levels were found to exceed that of the native promoter. Conversely, minimal eGFP expression was observed when this mutation was not in-frame, suggesting potential use of uORFs to regulate expression. Findings from this work will aid future improvements to the BEVS and will be particularly useful for those seeking to improve co-expression protocols.
Cited by 0Open access
Jeong Hyun Seo, Lin Li, Joo Sang Yeo et al. · Biotechnology and Bioengineering · 2003
Baculoviral polyhedrin, which originated from Autographa californica nuclear polyhedrosis virus (AcNPV), was employed for the first time as a novel fusion partner for expression of foreign proteins in an Escherichia coli system. We characterized the expression of recombinant polyhedrin protein fused to green fluorescent protein (GFP). The polyhedrin fusion protein ( approximately 58 kDa) was successfully expressed as an insoluble inclusion body comprising approximately 30% of the total cellular protein. The E. coli expressing polyhedrin-GFP fusion protein showed higher cell growth ( approximately 1.8-fold) and higher GFP yield ( approximately 3.5-fold) than the strain expressing soluble single GFP. Interestingly, the polyhedrin fusion portion showed almost the same characteristics as the native baculoviral polyhedrin; it was rapidly solubilized under alkaline conditions, similar to the conditions found in the insect midgut. In addition, the polyhedrin fusion portion was rapidly digested by alkaline proteases in insect Plutella xylostella midgut as well as by alpha-chymotrypsin, a protease that has similar properties to insect midgut polyhedra-associated alkaline proteases. These unique properties suggest that baculoviral polyhedrin might be an advantageous fusion partner for production of foreign proteins, especially harmful proteins, in E. coli expression systems.
Cited by 16