Journal: medRxiv

Article Title: Mucosal IgA to pre-fusion F protein predicts protection from RSV infection in a high burden setting

doi: 10.64898/2026.03.16.26348479

Figure Lengend Snippet: (A) Longitudinal trajectories of serum IgG (top row) and mucosal IgA (bottom row) antibody responses against four RSV-B proteins (PreF, PostF, G, NP) over time. Individual participant trajectories are shown as thin lines with low opacity, colored by infection status: not infected (black), sero-detected infections (orange), and PCR-confirmed infections (green). (B) Mean fold-change in antibody titres between the first bleed (pre-epidemic baseline) and second bleed (post-epidemic) for serum IgG and mucosal IgA responses to RSV-B proteins. Bars represent mean fold-change (log10 scale) stratified by infection status, with error bars indicating standard error.

Article Snippet: RSV antigens (RSV-A Pre-Fusion (ProteoGenix, product code: PX-P6126), RSV-B Pre-Fusion (SinoBiological, product code: 40832-V08B), RSV-A Post-Fusion (SinoBiological, product code: 11049-V08B), RSV-B Post-Fusion (SinoBiological, product code: 40999-V08H), RSV-A G protein (SinoBiological, product code: 11070-V08H2), RSV-B G protein (SinoBiological, product code: 13029-V08H, RSV-A Nucleoprotein (SinoBiological, product code: 40821-V08E and RSV-B Nucleoprotein (SinoBiological, product code: 40822-V08F)), were coupled to distinct bead regions.

Techniques: Infection

Journal: medRxiv

Article Title: Mucosal IgA to pre-fusion F protein predicts protection from RSV infection in a high burden setting

doi: 10.64898/2026.03.16.26348479

Figure Lengend Snippet: (A) Post-infection longitudinal antibody titers for four viral RSV-B proteins (PreF, PostF, G, and NP) across different antibody types; serum IgG and mucosal IgA. Lines show the median posterior predictive fit from the fitted Bayesian model, and the points show the observational titre data, with the size correlating with the sample size for that bin. (B) Peak antibody (x axis) and persistence measured as duration above a 2-fold (left panel) and 4-fold titre rise (right panel) in days. Data points show median posterior values for measurements of four viral RSV-B proteins (PreF, PostF, G, and NP) across different antibody types: serum IgG and mucosal IgA.

Article Snippet: RSV antigens (RSV-A Pre-Fusion (ProteoGenix, product code: PX-P6126), RSV-B Pre-Fusion (SinoBiological, product code: 40832-V08B), RSV-A Post-Fusion (SinoBiological, product code: 11049-V08B), RSV-B Post-Fusion (SinoBiological, product code: 40999-V08H), RSV-A G protein (SinoBiological, product code: 11070-V08H2), RSV-B G protein (SinoBiological, product code: 13029-V08H, RSV-A Nucleoprotein (SinoBiological, product code: 40821-V08E and RSV-B Nucleoprotein (SinoBiological, product code: 40822-V08F)), were coupled to distinct bead regions.

Techniques: Infection

Journal: medRxiv

Article Title: Mucosal IgA to pre-fusion F protein predicts protection from RSV infection in a high burden setting

doi: 10.64898/2026.03.16.26348479

Figure Lengend Snippet: Serum IgG, top row; mucosal IgA, bottom row and columns are viral antigen target (PreF, PostF, G, and NP for both RSV-A and RSV-B strains). The solid green line represents the mean estimated probability of protection given exposure to infection as a function of antibody titre, with shaded ribbons indicating 95% credible intervals. Background histograms show the distribution of antibody titres at infection for infected individuals (orange) versus non-infected individuals (gray).

Article Snippet: RSV antigens (RSV-A Pre-Fusion (ProteoGenix, product code: PX-P6126), RSV-B Pre-Fusion (SinoBiological, product code: 40832-V08B), RSV-A Post-Fusion (SinoBiological, product code: 11049-V08B), RSV-B Post-Fusion (SinoBiological, product code: 40999-V08H), RSV-A G protein (SinoBiological, product code: 11070-V08H2), RSV-B G protein (SinoBiological, product code: 13029-V08H, RSV-A Nucleoprotein (SinoBiological, product code: 40821-V08E and RSV-B Nucleoprotein (SinoBiological, product code: 40822-V08F)), were coupled to distinct bead regions.

Techniques: Infection

Journal: medRxiv

Article Title: Mucosal IgA to pre-fusion F protein predicts protection from RSV infection in a high burden setting

doi: 10.64898/2026.03.16.26348479

Figure Lengend Snippet: Model performance comparison across single biomarker models and the dual biomarker model, defined by out-of-sample predictive accuracy (LOO-ELPD, x-axis) and discrimination ability (area under the ROC curve, AUC, y-axis). Circles indicate serum IgG models, squares represent mucosal IgA models, and the triangle denotes the dual biomarker model combining serum IgG and mucosal IgA to RSV-B PreF. The best-performing model within each biomarker class is highlighted with darker shading. Error bars show the standard error of LOO-ELPD (horizontal) and 95% confidence intervals for AUC (vertical). The dashed horizontal line indicates an AUC of 0.7.

Article Snippet: RSV antigens (RSV-A Pre-Fusion (ProteoGenix, product code: PX-P6126), RSV-B Pre-Fusion (SinoBiological, product code: 40832-V08B), RSV-A Post-Fusion (SinoBiological, product code: 11049-V08B), RSV-B Post-Fusion (SinoBiological, product code: 40999-V08H), RSV-A G protein (SinoBiological, product code: 11070-V08H2), RSV-B G protein (SinoBiological, product code: 13029-V08H, RSV-A Nucleoprotein (SinoBiological, product code: 40821-V08E and RSV-B Nucleoprotein (SinoBiological, product code: 40822-V08F)), were coupled to distinct bead regions.

Techniques: Comparison, Biomarker Discovery

Journal: Mucosal immunology

Article Title: Respiratory syncytial virus activates epidermal growth factor receptor to suppress interferon regulatory factor 1-dependent interferon-lambda and antiviral defense in airway epithelium

doi: 10.1038/mi.2017.120

Figure Lengend Snippet: (A) BEAS-2b cells were treated with UV-inactivated RSV (UV RSV MOI 1; filled columns) (n=5 independent experiments, mean ± SEM; *** p<0.0001 vs. UV RSV). (B) NADPH activity was measured in BEAS-2b cells at 2 h. Cells were treated with serum-free medium alone (Control, empty columns), DPI (3 μM) alone, with UV RSV (MOI 1; filled columns) alone, or with the addition of DPI (n=3–6 independent experiments, mean ± SEM; ** p<0.005 vs. control; ### p<0.005 vs. UV RSV alone). (C) BEAS-2b cells were treated with serum-free medium alone (empty columns), Poly I:C alone (Poly I:C 100 μg/mL; filled colums), and Poly I:C plus RSV F protein (F protein 20 μg/mL; filled columns), and IRF-1 mRNA was analyzed by quantitative RT-PCR (n=6 independent experiments; *** p<0.0001 vs. serum-free medium; ### p<0.001 vs. RSV alone).

Article Snippet: RSV F protein was obtained from Sino Biological (Beijing, China).

Techniques: Activity Assay, Quantitative RT-PCR

Journal: PLoS ONE

Article Title: Discovery and Characterization of Phage Display-Derived Human Monoclonal Antibodies against RSV F Glycoprotein

doi: 10.1371/journal.pone.0156798

Figure Lengend Snippet: A shotgun mutagenesis alanine scanning library was constructed for the RSV F protein. The library contains 368 individual mutations at residues identified as surface exposed on the prefusion and postfusion forms of RSV F proteins. Each well of the mutation array plate contained one mutant with a defined substitution. (A) Reactivity results from a representative assay are shown with four positive (wildtype RSV F) and four negative (mock-transfected) control wells included on the plate. (B) Human HEK293T cells expressing the RSV F mutation library were tested for immunoreactivity with mAb 2E1, measured on an Intellicyt high-throughput flow cytometer. Clones with reactivity of <20% relative to that of wildtype RSV F (horizontal line) yet >70% reactivity for a control mAb (vertical line) were initially identified to be critical for mAb 2E1 binding (red dots), and were verified using algorithms described elsewhere . (C) Mutation of four individual residues reduced 2E1 binding (red bars) but not the binding of D25 and palivizumab (gray bars). Error bars represent range (half of the maximum minus minimum values) of at least two replicate data points. (D) Mutation of three individual residues reduced 3B1 binding (red bars) but not the binding of D25 and palivizumab (gray bars). Error bars represent range of at least two replicate data points.

Article Snippet: We have isolated a panel of RSV F protein specific human monoclonal antibodies from Morphosys HuCAL GOLD ® phage libraries by panning against RSV prefusion and postfusion F proteins and identified mAbs specifically against prefusion F and/or postfusion F proteins.

Techniques: Mutagenesis, Construct, Transfection, Control, Expressing, High Throughput Screening Assay, Flow Cytometry, Clone Assay, Binding Assay