ArticleFrontiers in microbiology2011
The Structure of the Hantavirus Zinc Finger Domain is Conserved and Represents the Only Natively Folded Region of the Gn Cytoplasmic Tail.
Article in Frontiers in microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Exploring the dynamics and interactions of the N-myc transactivation domain through solution nuclear magnetic resonance spectroscopy.The Biochemical journal · 2024Article
- Do NSm Virulence Factors in theViruses · 2024Article
- Nuclear Magnetic Resonance Spectroscopy to Study Virus Structure.Sub-cellular biochemistry · 2024Review
- Review
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- Recent Advances in Bunyavirus Glycoprotein Research: Precursor Processing, Receptor Binding and Structure.Viruses · 2021Review
- Amplicon-Based, Next-Generation Sequencing Approaches to Characterize Single Nucleotide Polymorphisms ofFrontiers in cellular and infection microbiology · 2020Article
- Self-association and subcellular localization of Puumala hantavirus envelope proteins.Scientific reports · 2019Article
- Hantavirus entry: Perspectives and recent advances.Advances in virus research · 2019Article
- Effect of solvent and protein dynamics in ligand recognition and inhibition of aminoglycoside adenyltransferase 2″-Ia.Protein science : a publication of the Protein Society · 2017Article
- RNA Encapsidation and Packaging in the Phleboviruses.Viruses · 2016Review
- A Molecular-Level Account of the Antigenic Hantaviral Surface.Cell reports · 2016Article
- Hantaviral Proteins: Structure, Functions, and Role in Hantavirus Infection.Frontiers in microbiology · 2015Review
- Hantavirus Gn and Gc envelope glycoproteins: key structural units for virus cell entry and virus assembly.Viruses · 2014Review
- Structural biology for virus research.Frontiers in microbiology · 2012Article
- An assembly model of rift valley Fever virus.Frontiers in microbiology · 2012Article
- Novel therapeutic approaches towardIndian journal of pharmacologyArticle
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Authors and funding
4 authors.
Funding
Abstract
Hantaviruses, of the family Bunyaviridae, are present throughout the world and cause a variety of infections ranging from the asymptomatic to mild and severe hemorrhagic fevers. Hantaviruses are enveloped anti-sense RNA viruses that contain three genomic segments that encode for a nucleocapsid protein, two membrane glycoproteins (Gn and Gc), and an RNA polymerase. Recently, the pathogenicity of hantaviruses has been mapped to the carboxyl end of the 150 residue Gn cytoplasmic tail. The Gn tail has also been shown to play a role in binding the ribonucleoprotein (RNP), a step critical for virus assembly. In this study, we use NMR spectroscopy to compare the structure of a Gn tail zinc finger domain of both a pathogenic (Andes) and a non-pathogenic (Prospect Hill) hantavirus. We demonstrate that despite a stark difference in the virulence of both of these viruses, the structure of the Gn core zinc finger domain is largely conserved in both strains. We also use NMR backbone relaxation studies to demonstrate that the regions of the Andes virus Gn tail immediately outside the zinc finger domain, sites known to bind the RNP, are disordered and flexible, thus intimating that the zinc finger domain is the only structured region of the Gn tail. These structural observations provide further insight into the role of the Gn tail during viral assembly as well as its role in pathogenesis.
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