ArticleJournal of virology2005
The hantavirus nucleocapsid protein recognizes specific features of the viral RNA panhandle and is altered in conformation upon RNA binding.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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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
48 citing papers in PubMed, 79 citations in OpenAlex.
- Characterization of minigenome systems for Hantaan and Seoul hantaviruses.Virus research · 2026Article
- Structural flexibility in the ordered domain of the dengue virus strain 2 capsid protein is critical for chaperoning viral RNA replication.Cellular and molecular life sciences : CMLS · 2025Article
- Puumala orthohantavirus: prevalence, biology, disease, animal models and recent advances in therapeutics development and structural biology.Frontiers in immunology · 2025Review
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- Information Encoded by the Flavivirus Genomes beyond the Nucleotide Sequence.International journal of molecular sciences · 2021Review
- A Novel Bunyavirus Discovered in Oriental Shrimp (Frontiers in microbiology · 2021Article
- Application of Aptamer-Based Assays to the Diagnosis of Arboviruses Important for Public Health in Brazil.International journal of molecular sciences · 2020Review
- Article
- Biodefense Implications of New-World Hantaviruses.Frontiers in bioengineering and biotechnology · 2020Review
- The nucleocapsid protein of hantaviruses: much more than a genome-wrapping protein.Virus genes · 2018Review
- Crimean-Congo hemorrhagic fever virus nucleocapsid protein has dual RNA binding modes.PloS one · 2017Article
- Homology modeling and molecular dynamics provide structural insights into tospovirus nucleoprotein.BMC bioinformatics · 2016Article
- RNA Encapsidation and Packaging in the Phleboviruses.Viruses · 2016Review
- Crystal Structure of the Core Region of Hantavirus Nucleocapsid Protein Reveals the Mechanism for Ribonucleoprotein Complex Formation.Journal of virology · 2016Article
- Inhibition of Rift Valley fever virus replication and perturbation of nucleocapsid-RNA interactions by suramin.Antimicrobial agents and chemotherapy · 2014Article
- Retrospective on the all-in-one retroviral nucleocapsid protein.Virus research · 2014Review
- Ribosomal protein S19-binding domain provides insights into hantavirus nucleocapsid protein-mediated translation initiation mechanism.The Biochemical journal · 2014Article
- Comparative nucleic acid chaperone properties of the nucleocapsid protein NCp7 and Tat protein of HIV-1.Virus research · 2012Review
- Identification of Rift Valley fever virus nucleocapsid protein-RNA binding inhibitors using a high-throughput screening assay.Journal of biomolecular screening · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hantaviruses are tripartite negative-sense RNA viruses and members of the Bunyaviridae family. The nucleocapsid (N) protein is the principal structural component of the viral capsid. N forms a stable trimer that specifically recognizes the panhandle structure formed by the viral RNA termini. We used trimeric glutathione S-transferase (GST)-N protein and small RNA panhandles to examine the requirements for specific recognition by Sin Nombre hantavirus N. Trimeric GST-N recognizes the panhandles of the three viral RNAs (S, M, and L) with high affinity, whereas the corresponding plus-strand panhandles of the complementary RNA are recognized with lower affinity. Based on analysis of nucleotide substitutions that alter either the higher-order structure of the panhandle or the primary sequence of the panhandle, both secondary structure and primary sequence are necessary for stable interaction with N. A panhandle 23 nucleotides long is necessary and sufficient for high-affinity binding by N, and stoichiometry calculations indicate that a single N trimer interacts with a single panhandle. Surprisingly, displacement of the panhandle structure away from the terminus does not eliminate recognition by N. The binding of N to the panhandle is an entropy-driven process resulting in initial stable N-RNA interaction followed by a conformational change in N. Taken together, these data provide insight into the molecular events that take place during interaction of N with the panhandle and suggest that specific high-affinity interaction between an RNA binding domain of trimeric N and the panhandle is required for encapsidation of the three viral RNAs.
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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 Socratic graph.