ArticlePloS one2013
Cryo-EM structure of a novel calicivirus, Tulane virus.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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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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Who cites it
23 citing papers in PubMed, 37 citations in OpenAlex.
- Navigating Uncertainties in RT-qPCR and Infectivity Assessment of Norovirus.Food and environmental virology · 2025Article
- Conformational Flexibility in Capsids Encoded by theViruses · 2024Review
- Evaluating the Potential of Ozone Microbubbles for Inactivation of Tulane Virus, a Human Norovirus Surrogate.ACS omega · 2024Article
- The 2.6 Å Structure of a Tulane Virus Variant with Minor Mutations Leading to Receptor Change.Biomolecules · 2024Article
- Impacts of Surface Characteristics and Dew Point on the Blue-Light (BLMicroorganisms · 2023Article
- Efficacy of EPA-registered disinfectants against two human norovirus surrogates and Clostridioides difficile endospores.Journal of applied microbiology · 2022Article
- Inactivation Mechanism and Efficacy of Grape Seed Extract for Human Norovirus Surrogate.Applied and environmental microbiology · 2022Article
- Expression of quasi-equivalence and capsid dimorphism in the Hepadnaviridae.PLoS computational biology · 2020Article
- Dynamics in the murine norovirus capsid revealed by high-resolution cryo-EM.PLoS biology · 2020Article
- Evaluation of Assays to Quantify Infectious Human Norovirus for Heat and High-Pressure Inactivation Studies Using Tulane Virus.Food and environmental virology · 2017Article
- Critical role of RIG-I and MDA5 in early and late stages of Tulane virus infection.The Journal of general virology · 2017Article
- Vesivirus 2117 capsids more closely resemble sapovirus and lagovirus particles than other known vesivirus structures.The Journal of general virology · 2017Article
- Antibody-Based Affinity Cryoelectron Microscopy at 2.6-Å Resolution.Structure (London, England : 1993) · 2016Article
- An algorithm for estimation and correction of anisotropic magnification distortion of cryo-EM images without need of pre-calibration.Journal of structural biology · 2016Article
- Antibody-based affinity cryo-EM grid.Methods (San Diego, Calif.) · 2016Article
- Mechanism of Cell Culture Adaptation of an Enteric Calicivirus, the Porcine Sapovirus Cowden Strain.Journal of virology · 2016Article
- Antigenic and Cryo-Electron Microscopy Structure Analysis of a Chimeric Sapovirus Capsid.Journal of virology · 2015Article
- Tulane virus recognizes sialic acids as cellular receptors.Scientific reports · 2015Article
- Tulane virus recognizes the A type 3 and B histo-blood group antigens.Journal of virology · 2015Article
- Role of histo-blood group antigens in primate enteric calicivirus infections.World journal of virology · 2014Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Tulane virus (TV) is a newly isolated cultivatable calicivirus that infects juvenile rhesus macaques. Here we report a 6.3 Å resolution cryo-electron microscopy structure of the TV virion. The TV virion is about 400 Å in diameter and consists of a T = 3 icosahedral protein capsid enclosing the RNA genome. 180 copies of the major capsid protein VP1 (∼57 KDa) are organized into two types of dimers A/B and C/C and form a thin, smooth shell studded with 90 dimeric protrusions. The overall capsid organization and the capsid protein fold of TV closely resemble that of other caliciviruses, especially of human Norwalk virus, the prototype human norovirus. These close structural similarities support TV as an attractive surrogate for the non-cultivatable human noroviruses. The most distinctive feature of TV is that its C/C dimers are in a highly flexible conformation with significantly reduced interactions between the shell (S) domain and the protruding (P) domain of VP1. A comparative structural analysis indicated that the P domains of TV C/C dimers were much more flexible than those of other caliciviruses. These observations, combined with previous studies on other caliciviruses, led us to hypothesize that the enhanced flexibility of C/C dimer P domains are likely required for efficient calicivirus-host cell interactions and the consequent uncoating and genome release. Residues in the S-P1 hinge between the S and P domain may play a critical role in the flexibility of P domains of C/C dimers.
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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.