ArticleJournal of virology1999
Multimers formed by the rotavirus nonstructural protein NSP2 bind to RNA and have nucleoside triphosphatase activity.
Article in Journal of virology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
60 citing papers in PubMed, 129 citations in OpenAlex.
- Serological responses to rotavirus NSP2 following administration of RV3-BB human neonatal rotavirus vaccine.Human vaccines & immunotherapeutics · 2018Trial
- K294E change in the rotavirus factory forming protein NSP2 stabilizes a rare C-terminal conformation.Journal of biomolecular structure & dynamics · 2026Article
- Comparative analysis of NSP5/VP2-induced viroplasm-like structures in rotavirus species A to J.Journal of virology · 2025Article
- Characterization of viroplasm-like structures by co-expression of NSP5 and NSP2 across rotavirus species A to J.Journal of virology · 2024Article
- Review
- The Role of the Host Cytoskeleton in the Formation and Dynamics of Rotavirus Viroplasms.Viruses · 2024Review
- The recruitment of TRiC chaperonin in rotavirus viroplasms correlates with virus replication.mBio · 2024Article
- Cryo-EM structure of rotavirus B NSP2 reveals its unique tertiary architecture.Journal of virology · 2024Article
- Principles of RNA recruitment to viral ribonucleoprotein condensates in a segmented dsRNA virus.eLife · 2023Article
- Structural basis of rotavirus RNA chaperone displacement and RNA annealing.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Review
- Plasmid-based reverse genetics for probing phosphorylation-dependent viroplasm formation in rotaviruses.Virus research · 2021Review
- A Genetically Engineered Rotavirus NSP2 Phosphorylation Mutant Impaired in Viroplasm Formation and Replication Shows an Early Interaction between vNSP2 and Cellular Lipid Droplets.Journal of virology · 2020Article
- Understanding the penetrance of intrinsic protein disorder in rotavirus proteome.International journal of biological macromolecules · 2020Article
- Coding-Gene Coevolution Analysis of Rotavirus Proteins: A Bioinformatics and Statistical Approach.Genes · 2019Article
- Phosphorylation cascade regulates the formation and maturation of rotaviral replication factories.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Single-Particle Detection of Transcription following Rotavirus Entry.Journal of virology · 2017Article
- RNA chaperones encoded by RNA viruses.Virologica Sinica · 2015Review
- Article
- A cypovirus VP5 displays the RNA chaperone-like activity that destabilizes RNA helices and accelerates strand annealing.Nucleic acids research · 2014Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The nonstructural protein NSP2 is a component of rotavirus replication intermediates and accumulates in cytoplasmic inclusions (viroplasms), sites of genome RNA replication and the assembly of subviral particles. To better understand the structure and function of the protein, C-terminally His-tagged NSP2 was expressed in bacteria and purified to homogeneity. In its purified form, the protein did not exist as a monomer but rather was present as an 8S-10S homomultimer consisting of 6 +/- 2 subunits of recombinant NSP2 (rNSP2). As shown by gel mobility shift assays, the rNSP2 multimers bound to RNA in discrete cooperative steps to form higher-order RNA-protein complexes. The RNA-binding activity of the rNSP2 multimers was determined to be nonspecific and to have a strong preference for single-stranded RNA over double-stranded RNA, for which it displayed little affinity. Enzymatic analysis revealed that rNSP2 possessed an associated nucleoside triphosphatase (NTPase) activity in vitro, which in the presence of Mg(2+) catalyzed the hydrolysis of each of the four NTPs to NDPs with equal efficiency. Evidence indicating that the hydrolysis of NTP resulted in the covalent linkage of the gamma-phosphate to rNSP2 was obtained. Additional experiments showed that NSP2 expressed transiently in MA014 cells is phosphorylated. We propose that NSP2 functions as a molecular motor, catalyzing the packaging of viral mRNA into core-like replication intermediates through the energy derived from its NTPase activity.
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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.