Effect of CSC against laboratory hCoV-229E strain at different time points.

Effect of CSC against laboratory hCoV-229E strain at different time points.</p

Effect of CSC on the infectivity of hCoV 229E was exposed to CSC surface and the samples were collected at each time point and titrated in MRC-5 cells.

The results shown are representative of duplicates. Control groups (steel, copper and sterile polystyrene) were treated identically at each time point. Samples were titrated in MRC-5 cells using four replicates. The dotted line denotes the limit of detection of the assay.</p

Effect of CSC in inactivating hCoV 229E compared to the sterile polystyrene group.

The inactivation log change value was calculated by subtracting the TCID50 value of sterile polystyrene from TCID50 value of CSC group collected at each time point. The dotted line denotes the limit of detection.</p

The effectiveness of CSC against SARS-CoV-2 in clinical samples by RT-qPCR.

The effectiveness of CSC against SARS-CoV-2 in clinical samples by RT-qPCR.</p

Primers and probes for RT-qPCR.

Primers and probes for RT-qPCR.</p

Additional file 2: of A next generation sequencing-based method to study the intra-host genetic diversity of norovirus in patients with acute and chronic infection

Various supporting data. This file contains: 1) the data used to estimate the correlation between percentage of NoVreads and Ct values, 2) the commands used for NGS analysis, 3) a summary of the sequences filtered out by Prinseq-lite due to quality control and 4) a description of the primers designed for sequencing sample OU3 via Sanger's method. (DOCX 86 kb

Antigenic Relatedness of Norovirus GII.4 Variants Determined by Human Challenge Sera

<div><p>The GII.4 noroviruses (NoVs) are a single genotype that is responsible for over 50% of NoV gastroenteritis epidemics worldwide. However, GII.4 NoVs have been found to undergo antigenic drifts, likely selected by host herd immunity, which raises an issue for vaccine strategies against NoVs. We previously characterized GII.4 NoV antigenic variations and found significant levels of antigenic relatedness among different GII.4 variants. Further characterization of the genetic and antigenic relatedness of recent GII.4 variants (2008b and 2010 cluster) was performed in this study. The amino acid sequences of the receptor binding interfaces were highly conserved among all GII.4 variants from the past two decades. Using serum samples from patients enrolled in a GII.4 virus challenge study, significant cross-reactivity between major GII.4 variants from 1998 to 2012 was observed using enzyme-linked immunosorbent assays and HBGA receptor blocking assays. The overall abilities of GII.4 NoVs to bind to the A/B/H HBGAs were maintained while their binding affinities to individual ABH antigens varied. These results highlight the importance of human HBGAs in NoV evolution and how conserved antigenic types impact vaccine development against GII.4 variants.</p></div

The antibodies from mice immunized with P particles from the 2008b and 2010 clusters blocked GII.4 P particle (VA387, 98Y96C) binding to A-, B-type saliva, and H type 3 oligosaccharide.

<p>VA387 P particles were blocked with mouse antisera against each of the five strains (2007Y2008bC, 2010Y2008bC, 2011Y2010C4, 2012Y2010C2, and 98Y96C). The y-axis indicates the serum dilution (blockade titer) as determined from optical density values. The blue bars indicate the antiserum titer at which 50% of the binding was blocked (BT₅₀) compared to unblocked controls and red bars indicate the titer at which 90% of the binding was blocked (BT₉₀). The results are averaged from at least two independent experiments.</p

Phylogenetic tree of GII.4 norovirus P domain sequences.

<p>Multiple alignments were generated using 82 P domain amino acid sequences with MegAlign Lasergene software and the phylogenetic tree was generated using the neighbor-joining method in MEGA (version 4.1). GII.4 sequences from 1974 to 2012 grouping in different clusters are labeled. Strains isolated in this study are as follows: 2005Y2004C, 2006Y2004C, 2006Y2006aC, 2007Y2006bC, 2008Y2006bC1, 2008Y2006bC2, 2008Y2006bC3, 2008Y2008aC1, 2007Y2008bC, 2010Y2008bC, 2010Y2010C1, 2010Y2010C2, 2011Y2010C1, 2011Y2010C2, 2011Y2010C3, 2011Y2010C4, 2012Y2010C1, and 2012Y2010C2. These strains are highlighted by a solid black triangle.</p

Binding of GII.4 P particles to human saliva samples.

<p>Boiled saliva samples were coated onto 96-well plates prior to the addition of P particlesfrom ten GII.4 viruses expressed in this study (2005Y2004C, 2006Y2004C, 2007Y2006bC, 2007Y2008bC, 2010Y2008bC, 2010Y2010C1, 2011Y2010C1, 2011Y2010C4, 2012Y2010C1, and 2012Y2010C2). The P particles were tested in a series of 3-fold dilutions by enzyme-linked immunosorbent assay (ELISA) (optical densities at 450 nm were averaged from at least three independent experiments) and the 98Y96C (VA387) P particle was set as the positive control for binding. “O,” “A,” “B,” and “N” represent the type O (H antigen), A, B, and nonsecretor saliva, respectively.</p