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Updated: Mar 29, 2026

Protein Transfection of Mouse Lung
Published on: May 15, 2013
African Swine Fever Virus R238L and R298L Disrupt Lung Cell Collagen Formation and Cell Adhesion Pathway by Targeting
Siqi Niu1, Fanghong Zhang1, Jingchun Wen1
1College of Animal Science and Technology, Yangtze University, Jingzhou 434025, China.
Abstract:
The regulatory mechanisms of collagen formation and cell adhesion pathways during African Swine Fever Virus (ASFV) infection remain poorly understood. This study aims to investigate whether ASFV manipulates these pathways by targeting host transcriptional regulators. Through weighted Kendall correlation analysis of transcription factor binding sites (TFBSs) in differentially expressed genes (DEGs) from the lung tissue of ASFV-recovered pigs, we identified SP2 and KLF6 as key transcription factors (TFs) associated with collagen synthesis and cell adhesion, respectively. Domain-domain interaction prediction, followed by Förster resonance energy transfer (FRET) assays, confirmed that the ASFV proteins R238L and R298L directly bind to the zf-C2H2 domains of SP2 and KLF6. Furthermore, overexpression of R238L and R298L in HeLa and 3D4/21 cells significantly downregulated SP2 and KLF6 target genes involved in these pathways. Our findings reveal a novel mechanism by which ASFV proteins R238L and R298L interfere with host transcription factors SP2 and KLF6, potentially disrupting collagen matrix integrity and cell adhesion to facilitate viral pathogenesis.
Insights
African Swine Fever Virus (ASFV) infection disrupts collagen and cell adhesion by targeting host transcription factors. ASFV proteins R238L and R298L bind SP2 and KLF6, downregulating key genes.
Area of Science:
- Virology
- Molecular Biology
- Cellular Biology
Background:
- African Swine Fever Virus (ASFV) infection impacts collagen formation and cell adhesion pathways.
- The precise regulatory mechanisms and host targets involved in ASFV pathogenesis are not fully understood.
Purpose of the Study:
- To investigate if ASFV manipulates host collagen synthesis and cell adhesion pathways by targeting transcriptional regulators.
- To identify specific ASFV proteins and host factors involved in this interaction.
Main Methods:
- Weighted Kendall correlation analysis of transcription factor binding sites (TFBSs) in differentially expressed genes (DEGs) from ASFV-infected pig lung tissue.
- Domain-domain interaction prediction and Förster resonance energy transfer (FRET) assays.
- Overexpression studies in HeLa and 3D4/21 cell lines.
Main Results:
- SP2 and KLF6 were identified as key transcription factors (TFs) regulating collagen synthesis and cell adhesion, respectively.
- ASFV proteins R238L and R298L were found to directly bind to SP2 and KLF6.
- Overexpression of R238L and R298L led to downregulation of SP2 and KLF6 target genes.
Conclusions:
- ASFV proteins R238L and R298L interfere with host transcription factors SP2 and KLF6.
- This interaction potentially disrupts collagen matrix integrity and cell adhesion, facilitating ASFV pathogenesis.
- Reveals a novel viral mechanism impacting host cellular processes.
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