Norovirus assembly and stability

Pogan, Ronja; Dülfer, Jasmin; Uetrecht, Charlotte

doi:10.1016/j.coviro.2018.05.003

Cited by 45 publications

(36 citation statements)

References 60 publications

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“…Although norovirus VLPs have been thought to exist only in T = 3 assemblies, our cryo-EM VLP structures revealed structural polymorphism between and within genogroups in identical buffer conditions (15, 16). Our GI.1 structure is in good agreement with the previous GI.1 crystal structure (0.8-Å rmsd).…”

Section: Resultsmentioning

confidence: 79%

High-resolution cryo-EM structures of outbreak strain human norovirus shells reveal size variations

Jung

Grant

Thomas

et al. 2019

Proc. Natl. Acad. Sci. U.S.A.

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Noroviruses are a leading cause of foodborne illnesses worldwide. Although GII.4 strains have been responsible for most norovirus outbreaks, the assembled virus shell structures have been available in detail for only a single strain (GI.1). We present high-resolution (2.6- to 4.1-Å) cryoelectron microscopy (cryo-EM) structures of GII.4, GII.2, GI.7, and GI.1 human norovirus outbreak strain virus-like particles (VLPs). Although norovirus VLPs have been thought to exist in a single-sized assembly, our structures reveal polymorphism between and within genogroups, with small, medium, and large particle sizes observed. Using asymmetric reconstruction, we were able to resolve a Zn2+metal ion adjacent to the coreceptor binding site, which affected the structural stability of the shell. Our structures serve as valuable templates for facilitating vaccine formulations.

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Section: Resultsmentioning

confidence: 79%

High-resolution cryo-EM structures of outbreak strain human norovirus shells reveal size variations

Jung

Grant

Thomas

et al. 2019

Proc. Natl. Acad. Sci. U.S.A.

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“…Overlay of Fab A1227 onto the GI.1 capsid structure (Figures 4E and 4F) indicated that other P domains on the assembled norovirus capsid would clash with both heavy and light chains of the Fab, with only minor clashes with the shell domains (Figure 4G), suggesting that structural rearrangements of the P domain could either expose the A1227 binding site or allow binding at a neighboring P domain. Its lack of blockade or neutralizing activity likely results from antibody A1227 only recognizing defects or maturation intermediates (Pogan et al., 2018).…”

Section: Resultsmentioning

confidence: 99%

Sera Antibody Repertoire Analyses Reveal Mechanisms of Broad and Pandemic Strain Neutralizing Responses after Human Norovirus Vaccination

et al. 2019

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Summary Rapidly evolving RNA viruses, such as the GII.4 strain of human norovirus (HuNoV), and their vaccines elicit complex serological responses associated with previous exposure. Specific correlates of protection, moreover, remain poorly understood. Here, we report the GII.4-serological antibody repertoire—pre- and post-vaccination—and select several antibody clonotypes for epitope and structural analysis. The humoral response was dominated by GII.4-specific antibodies that blocked ancestral strains or by antibodies that bound to divergent genotypes and did not block viral-entry-ligand interactions. However, one antibody, A1431, showed broad blockade toward tested GII.4 strains and neutralized the pandemic GII.P16-GII.4 Sydney strain. Structural mapping revealed conserved epitopes, which were occluded on the virion or partially exposed, allowing for broad blockade with neutralizing activity. Overall, our results provide high-resolution molecular information on humoral immune responses after HuNoV vaccination and demonstrate that infection-derived and vaccine-elicited antibodies can exhibit broad blockade and neutralization against this prevalent human pathogen.

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“…Because of the lack of a good cell cultivation system for human norovirus, studies concerning norovirus stability have relied on the use of surrogates or recombinant capsids, as reviewed by Pogan et al (). MS2 are among the viruses that have been used as surrogates for norovirus.…”

Section: Resultsmentioning

confidence: 99%

Virus inactivation in groundwater in a postglacial lava field in arctic climate

Benediktsdóttir

Gunnarsdóttir

Ómarsdóttir

et al. 2020

Lett Appl Microbiol

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Outbreaks of viral gastroenteritis are often connected to contaminated drinking water. The assessment of the water quality relies on the cultivation of indicator bacteria, and little is known of the fate of viruses in groundwater, especially in arctic regions. In Iceland, the groundwater temperature is between 3 and 6°C. The aim of this study was to determine virus inactivation at low temperature in a groundwater microcosm and in a borehole in a postglacial lava field. Two phage species that are commonly used as surrogates for norovirus were used, MS2 and PhiX174. Dialysis bags were used for the samples, and a device was constructed to hold many samples at a time and protect the samples in the borehole. No significant decrease of infective PhiX174 phages in the borehole or of the MS2 phages in the microcosm was observed. A slightly significant decrease of PhiX174 in the microcosm was noticed, with one log reduction time of 476 days. On the other hand, a significant reduction in MS2 was found in the field test, where the time needed for 90% reduction was 12·5 days. The results showed that an infective virus can exist in groundwater for months or years in arctic regions and a great difference may exist between results from microcosm and field tests. Significance and Impact of the Study This study reveals that arctic regions are highly sensitive to virus contamination as an infective virus may exist in groundwater for years at low temperature. The results also show that the virus inactivation observed in field tests may differ considerably from the inactivation observed in laboratory microcosms. The results emphasize the importance of large protection zones around drinking water intakes as well as good wastewater treatment so that the likelihood of faecal contamination of groundwater is reduced.

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Norovirus assembly and stability

Cited by 45 publications

References 60 publications

High-resolution cryo-EM structures of outbreak strain human norovirus shells reveal size variations

High-resolution cryo-EM structures of outbreak strain human norovirus shells reveal size variations

Sera Antibody Repertoire Analyses Reveal Mechanisms of Broad and Pandemic Strain Neutralizing Responses after Human Norovirus Vaccination

Virus inactivation in groundwater in a postglacial lava field in arctic climate

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