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N460S on PB2 and I163T on nucleoprotein synergistically enhance the replication and pathogenicity of influenza B virus

ABSTRACT: N460S on PB2 and I163T on nucleoprotein synergistically enhance the replication and pathogenicity of influenza B virus

PROVIDER: PRJNA1223324 | ENA |

REPOSITORIES: ENA

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N460S on PB2 and I163T on nucleoprotein synergistically enhance the replication and pathogenicity of influenza B virus

Project description:Influenza B virus (IBV), though often overshadowed by influenza A viruses (IAVs), remains a significant global public health concern, particularly during seasons when it predominates. However, the molecular mechanisms underlying IBV pathogenicity remain largely unknown. In this study, we analyzed polymerase polymorphisms in an IBV isolated from a single patient’s oropharyngeal swab and identified two plaque colonies with distinct replication and pathogenicity phenotypes, associated with the PB2:N460S and NP:I163T substitutions. Using reverse genetics, we generated recombinant IBV mutants to evaluate the impact of these substitutions. The results showed that while neither mutation alone significantly affected viral replication or pathogenicity, their combination markedly enhanced both. Transcriptomic analysis of infected lung tissues revealed heightened immune activation, including upregulation of antiviral and immune-related genes, contributing to excessive inflammation and disease severity. Mechanistically, both substitutions increased protein expression and strengthened PB2-NP interaction, but only together did they enhance polymerase activity. Structural modeling suggested that PB2:460 is positioned at the PB2-NP interface, whereas NP:163 is not, indicating an indirect functional interplay. These findings provide new insights into the molecular determinants of IBV pathogenesis, highlighting the synergistic effect of PB2:N460S and NP:I163T in enhancing viral fitness and exacerbating disease outcomes.

2025-08-21 | GSE289500 | GEO

Project description:N460S on PB2 and I163T on nucleoprotein synergistically enhance the replication and pathogenicity of influenza B virus

| PRJNA1294812 | ENA

Compound mutations in HRC and MYBPC3 synergistically increase cardiac pathogenicity

Project description:Compound mutations in HRC and MYBPC3 synergistically increase cardiac pathogenicity

| PRJNA1174185 | ENA

Effect of p95HER2 overexpression on gene expression in PB2 mouse breast tumor xenografts.

Project description:To explore how p95HER2 regulates gene expression to promote tumor growth in immunocompetent mice, we engineered PB2 mouse breast cancer cells to express p95HER2 under the control of doxycycline. Both empty vector (EV) and p95HER2 cells were implanted to the mammary fat pads of immunocompetent C57BL/6 mice, which were placed under a DOX625 doxycycline diet. Tumor xenografts were harvested 3 weeks after inoculation. We then performed transcriptomic analysis using the RNA-seq data from PB2-EV and PB2-p95HER2 tumors.

2024-12-14 | GSE220203 | GEO

Limosilactobacillus reuteri strain:PB2

Project description:Limosilactobacillus reuteri strain:PB2 Genome sequencing and assembly

| PRJNA813581 | ENA

IM005 - Mouse infection with PB2-627E: A/Vietnam/1203-CIP048_RG2/2004 (H5N1)

Project description:To determine the host response (C57BL/6 mouse model) to the PB2-627E: A/Vietnam/1203-CIP048_RG2/2004 (H5N1) virus at 10^4 PFU.

2013-01-05 | GSE43301 | GEO

Leuconostoc suionicum strain:VITA-PB2

Project description:Leuconostoc suionicum strain:VITA-PB2 Genome sequencing

| PRJNA1169668 | ENA

Caballeronia sp. PB2 W CO

Project description:Caballeronia sp. PB2 W CO Genome sequencing

| PRJNA1212040 | ENA

Differential effects of p95HER2 and FL-HER2 on gene expression in PB2 mouse breast tumor xenografts at early and late stages.

Project description:To explore how p95HER2 regulates gene expression to promote tumor growth in immunocompetent mice, we engineered PB2 mouse breast cancer cells to express either p95HER2 or control FL-HER2 under the control of doxycycline. Both FL-HER2 and p95HER2 cells were implanted to the mammary fat pads of immunocompetent C57BL/6 mice that were placed under a DOX625 doxycycline diet. Tumor xenografts were harvested 10 and 22 days after inoculation. We then performed transcriptomic analysis using RNA-seq data from PB2-FL-HER2 and PB2-p95HER2 tumors.

2024-12-14 | GSE256132 | GEO

Influenza Polymerase Can Adopt an Alternative Configuration Involving a Radical Repacking of PB2 Domains

Project description:Influenza virus polymerase transcribes or replicates the segmented RNA genome (vRNA) into respectively viral mRNA or full-length copies and initiates RNA synthesis by binding the conserved 3' and 5' vRNA ends (the promoter). In recent structures of promoter-bound polymerase, the cap-binding and endonuclease domains are configured for cap snatching, which generates capped transcription primers. Here, we present a FluB polymerase structure with a bound complementary cRNA 5' end that exhibits a major rearrangement of the subdomains within the C-terminal two-thirds of PB2 (PB2-C). Notably, the PB2 nuclear localization signal (NLS)- containing domain translocates ~90 A ̊ to bind to the endonuclease domain. FluA PB2-C alone and RNA-free FluC polymerase are similarly arranged. Biophysical and cap-dependent endonuclease assays show that in solution the polymerase explores different conformational distributions depending on which RNA is bound. The inherent flexibility of the polymerase allows it to adopt alternative conformations that are likely important during polymerase maturation into active progeny RNPs.</br></br>Extra contact information:</br><a href="mailto:cusack@embl.fr">Stephen Cusack</a>, EMBL Grenoble Outstation, Unit of Virus Host-Cell Interactions, France ( corresponding author and lab head )

2016-01-04 | PXD002234 | Pride

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