ArticleProceedings of the National Academy of Sciences of the United States of America2003
Chaperone-mediated in vitro assembly of Polyomavirus capsids.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
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Who cites it
68 citing papers in PubMed, 151 citations in OpenAlex.
- Remodeling of the cellular membrane architecture in response to BK polyomavirus infection.Virology journal · 2026Review
- Mysteries of adenovirus packaging.Journal of virology · 2025Review
- Molecular mechanisms of the viral encoded chaperone 100K in capsid folding and assembly of adenovirus.Nature communications · 2025Article
- A pan-respiratory antiviral chemotype targeting a transient host multi-protein complex.Open biology · 2024Article
- Active viral infection during blooms of a dinoflagellate indicates dinoflagellate-viral co-adaptation.Applied and environmental microbiology · 2023Article
- Heat shock protein: a double-edged sword linking innate immunity and hepatitis B virus infection.Journal of virus eradication · 2023Review
- Serratia marcescens-S3 inhibits Potato virus Y by activating ubiquitination of molecular chaperone proteins NbHsc70-2 in Nicotiana benthamiana.Microbial biotechnology · 2022Article
- Heat shock cognate protein 70 is required for rice stripe tenuivirus accumulation and transmission in small brown planthopper.Archives of virology · 2022Article
- Heat shock protein 70 could enhance porcine epidemic diarrhoea virus replication by interacting with membrane proteins.Veterinary research · 2021Article
- Diversity in heat shock protein families: functional implications in virus infection with a comprehensive insight of their role in the HIV-1 life cycle.Cell stress & chaperones · 2021Review
- Comparative evaluation of integrated purification pathways for bacterial modular polyomavirus major capsid protein VP1 to produce virus-like particles using high throughput process technologies.Journal of chromatography. A · 2021Article
- Stress proteins: the biological functions in virus infection, present and challenges for target-based antiviral drug development.Signal transduction and targeted therapy · 2020Review
- Cold Exposure-Induced Up-Regulation of Hsp70 Positively Regulates PEDV mRNA Synthesis and Protein Expression In Vitro.Pathogens (Basel, Switzerland) · 2020Article
- Proteostasis in Viral Infection: Unfolding the Complex Virus-Chaperone Interplay.Cold Spring Harbor perspectives in biology · 2020Review
- Article
- Hsc70-2 is required for Beet black scorch virus infection through interaction with replication and capsid proteins.Scientific reports · 2018Article
- Virus-like particles vaccine containing Clonorchis sinensis tegumental protein induces partial protection against Clonorchis sinensis infection.Parasites & vectors · 2017Article
- Merkel cell polyomavirus and Merkel cell carcinoma.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Evidence that Hsc70 Is Associated with Cucumber Necrosis Virus Particles and Plays a Role in Particle Disassembly.Journal of virology · 2017Article
- Human Polyomaviruses: The Battle of Large and Small Tumor Antigens.Virology : research and treatment · 2017Review
8 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The polyomavirus coat protein viral protein 1 (VP1) has the intrinsic ability to self-assemble in vitro into polymorphic capsid-like structures on addition of calcium. In contrast, polyomavirus assembly in vivo is rigorously controlled, such that virions of uniform size are formed only in the cell nucleus. During viral infection, the 72 kDa cellular chaperone heat shock cognate protein (hsc70) binds VP1 posttranslation and colocalizes with VP1 to the nucleus, thereby suggesting a role for approximately 70-kDa heat shock protein (hsp70) family chaperones in regulating the quality and location of capsid assembly. We found that, after expression of recombinant VP1 in Escherichia coli, the prokaryotic hsp70 chaperone DnaK copurified with the VP1 C-terminal domain that links pentamers in an assembled capsid. When stably bound to VP1, DnaK inhibited in vitro assembly induced by calcium. However, in the presence of ATP, the hsp70 chaperone system comprised of DnaK, DnaJ, and GrpE assembled VP1 into uniform capsids without requiring calcium. Chaperone-mediated assembly was similarly catalyzed by the eukaryotic hsc70 protein, in combination with the J-domain function of the simian virus 40 large T-antigen protein. Thus, polyomavirus capsid assembly can be recapitulated with high-fidelity in vitro using either prokaryotic or eukaryotic hsp70 chaperone systems, thereby supporting a role for cellular chaperones in the in vivo regulation of virion assembly.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.