Characterization of self-assembled virus-like particles of human polyomavirus BK generated by recombinant baculoviruses

Li, Tiancheng; Takeda, Naokazu; Kato, Kenzo; Nilsson, Josefina; Li, Xing; Haag, Lars; Cheng, R. Holland; Miyamura, Tatsuo

doi:10.1016/s0042-6822(03)00141-7

Cited by 52 publications

(57 citation statements)

References 28 publications

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“…The BKPyV capsid structure consists of three proteins, VP1, VP2, and VP3. The major capsid protein, VP1, oligomerizes into pentamers during virion production and makes up the outer shell of the particle, with 72 pentamers stabilized by inter-and intra-disulfide bonds (10). It is believed that these disulfide bonds become reduced and/or isomerized by host disulfide reductases and isomerases when the virus infects a naive cell and traffics through the ER (9,11).…”

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confidence: 99%

Role of Cell-Type-Specific Endoplasmic Reticulum-Associated Degradation in Polyomavirus Trafficking

Bennett

Jiang

Imperiale

2013

J Virol

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BK polyomavirus (BKPyV) is a widespread human pathogen that establishes a lifelong persistent infection and can cause severe disease in immunosuppressed patients. BKPyV is a nonenveloped DNA virus that must traffic through the endoplasmic reticulum (ER) for productive infection to occur; however, it is unknown how BKPyV exits the ER before nuclear entry. In this study, we elucidated the role of the ER-associated degradation (ERAD) pathway during BKPyV intracellular trafficking in renal proximal tubule epithelial (RPTE) cells, a natural host cell. Using proteasome and ERAD inhibitors, we showed that ERAD is required for productive entry. Altered trafficking and accumulation of uncoated viral intermediates were detected by fluorescence in situ hybridization and indirect immunofluorescence in the presence of an inhibitor. Additionally, we detected a change in localization of partially uncoated virus within the ER during proteasome inhibition, from a BiP-rich area to a calnexin-rich subregion, indicating that BKPyV accumulated in an ER subcompartment. Furthermore, inhibiting ERAD did not prevent entry of capsid protein VP1 into the cytosol from the ER. By comparing the cytosolic entry of the related polyomavirus simian virus 40 (SV40), we found that dependence on the ERAD pathway for cytosolic entry varied between the polyomaviruses and between different cell types, namely, immortalized CV-1 cells and primary RPTE cells.

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confidence: 99%

Role of Cell-Type-Specific Endoplasmic Reticulum-Associated Degradation in Polyomavirus Trafficking

Bennett

Jiang

Imperiale

2013

J Virol

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“…It is a nonenveloped virus (ϳ50.0 nm in diameter) with a circular double-stranded DNA genome (ϳ5 kb). The capsid has icosahedral symmetry and is built of 72 capsomers that are all pentamers of the protein VP1 arranged in a Tϭ7 icosahedral lattice (21). All known polyomaviruses have three structural proteins (VP1, VP2, and VP3), of which VP1 is the major capsid protein.…”

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confidence: 99%

Structure and Assembly of a T =1 Virus-Like Particle in BK Polyomavirus

Nilsson

Miyazaki

et al. 2005

J Virol

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In polyomaviruses the pentameric capsomers are interlinked by the long C-terminal arm of the structural protein VP1. The T‫7؍‬ icosahedral structure of these viruses is possible due to an intriguing adaptability of this linker arm to the different local environments in the capsid. To explore the assembly process, we have compared the structure of two virus-like particles (VLPs) formed, as we found, in a calcium-dependent manner by the VP1 protein of human polyomavirus BK. The structures were determined using electron cryomicroscopy (cryo-EM), and the three-dimensional reconstructions were interpreted by atomic modeling. In the small VP1 particle, 26.4 nm in diameter, the pentameric capsomers form an icosahedral T‫1؍‬ surface lattice with meeting densities at the threefold axes that interlinked three capsomers. In the larger particle, 50.6 nm in diameter, the capsomers form a T‫7؍‬ icosahedral shell with three unique contacts. A folding model of the BKV VP1 protein was obtained by alignment with the VP1 protein of simian virus 40 (SV40). The model fitted well into the cryo-EM density of the T‫7؍‬ particle. However, residues 297 to 362 of the C-terminal arm had to be remodeled to accommodate the higher curvature of the T‫1؍‬ particle. The loops, before and after the C-terminal short helix, were shown to provide the hinges that allowed curvature variation in the particle shell. The meeting densities seen at the threefold axes in the T‫1؍‬ particle were consistent with the triple-helix interlinking contact at the local threefold axes in the T‫7؍‬ structure.The BK virus (BKV) is a human virus belonging to the Polyomaviridae family. It is a nonenveloped virus (ϳ50.0 nm in diameter) with a circular double-stranded DNA genome (ϳ5 kb). The capsid has icosahedral symmetry and is built of 72 capsomers that are all pentamers of the protein VP1 arranged in a Tϭ7 icosahedral lattice (21). All known polyomaviruses have three structural proteins (VP1, VP2, and VP3), of which VP1 is the major capsid protein. Overall amino acid sequence homology between BKV and the other human polyomavirus, JCV, is 75%, and that with the simian polyomavirus (SV40) is 69% (9). In the VP1 protein the sequence similarity rises to 77% and 74% for the JCV and SV40, respectively (35). Due to the high similarity, the solved atomic structure of VP1 of SV40 provides us a template to create a model of the BKV VP1 protein folding.The structures of the SV40 and murine polyomavirus have been determined and show similar features to that seen in the BKV (1, 12). The VP1 pentamer of SV40 and murine polyomavirus is built as a ring of five ␤-barrel-shaped VP1 monomers, tightly linked by interacting loops between the framework of ␤-strands (22,33,34,40). The C-terminal subdomain of each VP1 monomer "invades" a neighboring pentamer, thereby tying the pentamers together in the virion shell. There are six unique monomers building up the capsid (monomer ␣, ␣Ј, and ␣Љ at the local threefold; ␤, ␤Ј around the icosahedral threefold, and ␥ at the twofold) (34). The major s...

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“…For example, expression of human polyomavirus by recombinant baculovirus system resulted in VLPs that were able to induce only conformational antibodies when injected into rabbits. Both human and rabbit virus-specific antibodies failed to react with denatured viral antigens in dot blot and ELISA (Li et al, 2003). Joelson et al (1997) utilized antibodies produced by hyper-immunization of rabbits with denatured TBSV particles in order to detect the chimeric virus particles displaying human immunodeficiency virus epitopes in Western blots.…”

Section: Resultsmentioning

confidence: 99%

Creation and Over-Expression of Polyvalent Capsids Displaying Larger Segments of Ricin Achain as the Efficacious Vaccines of Ricin Toxin

Reddy¹

2006

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Characterization of self-assembled virus-like particles of human polyomavirus BK generated by recombinant baculoviruses

Cited by 52 publications

References 28 publications

Role of Cell-Type-Specific Endoplasmic Reticulum-Associated Degradation in Polyomavirus Trafficking

Role of Cell-Type-Specific Endoplasmic Reticulum-Associated Degradation in Polyomavirus Trafficking

Structure and Assembly of a T =1 Virus-Like Particle in BK Polyomavirus

Creation and Over-Expression of Polyvalent Capsids Displaying Larger Segments of Ricin Achain as the Efficacious Vaccines of Ricin Toxin

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