Fig 1: Comparison of the interaction of EGFR with RNase3 (R97 and T97), RNase5 and EGF by molecular modelling. a Primary sequence alignment of EGF, RNase3 and RNase5. The common interacting region is underlined. b Representative binding of EGFR with EGF, RNase5, and RNase3 single nucleotide polymorphisms: RNase3-R97 and RNase3-T97. The crystal complex of EGFR with EGF (PDB ID: 3NJP) is depicted. EGFR is coloured in grey, the protein ligands were coloured in pink, the interacting residues from EGFR and the ligands were coloured in blue and red, respectively
Fig 2: RNase3 inhibits bacterial and viral infection within macrophages. Overexpression of RNase3 in macrophage inhibits M. aurum and RSV proliferation. a the number of M. aurum inside of macrophage was counted by CFU assay and compared with wild-type THP1-induced macrophages (WT) and RNase3 overexpression THP1-induced macrophages (OX) for up to 3 days; b RSV was quantified by probe-qPCR, the intracellular RSV was normalized using GAPDH gene in WT and OX cells; c MTT assay was applied to measure the cell viability, 0 h WT group was used for normalization (100%); d Comparison of the relative transcriptional expression of RNase3 gene by qPCR using GAPDH as a reference. Cell viability and RNase3 expression was measured in WT, OX, WT infected with M. aurum (WT + M. aurum) or RSV (WT + RSV), and OX cells infected with M. aurum (OX + M. aurum) or RSV (OX + RSV) THP1-macrophage-derived cells; significance is indicated as *P < 0.05 and **P < 0.01
Fig 3: Schematic illustration of the proposed molecular mechanism of RNase3 modulation in human macrophage. The genes associated to RNase catalytic activity were labelled in red. EGFR epidermal growth factor receptor, IFIT interferon induced protein with tetratricopeptide repeats, EGR1 early growth response 1, JUN jun proto-oncogene or AP-1 transcription factor subunit, NFkB nuclear factor Kappa B, transcription regulator, STAT signal transducer and activator of transcription, IRF interferon regulatory factor, VCAM vascular cell adhesion molecule, MMP matrix metallopeptidase, TGF transforming growth factor, TNF tumour necrosis factor, TRAF TNF receptor-associated factor, IL interleukin, CCL C–C motif chemokine ligand, CXCL C-X-C motif chemokine ligand, ISG15 interferon induced 15 kDa protein, OAS 2'-5'-oligoadenylate synthetase, IFN interferon, PCNA proliferating cell nuclear antigen, CDK cyclin-dependent kinase, BRCA1 Breast Cancer gene 1, DNA repair associated gene
Fig 4: Necroptosis is correlated with neutrophilic inflammation in CRSwNP. (A and B) The protein levels of IL-8 and CXCL1 in tissue homogenates were detected by ELISA (n=22–24 per group). (C) Spearman correlations between IL-1a, HMGB1, IL-8, CXCL1 protein levels with p-MLKL positive cell numbers in control tissues and nasal polyps (n=28) (D) IHC staining of Myeloperoxidase (MPO), Neutrophil Elastase (NE) and Eosinophil Cationic Protein (ECP) in control tissues and nasal polyps. The positive cells were counted over high power field (400×) (n=15 per group). Scale bars: 50 µm. (E) Spearman correlations between MPO, NE or ECP positive cell numbers with p-MLKL positive cell numbers and in control tissues and nasal polyps (n=30). The data were shown as mean±SEM. *p<0.05, **p<0.01, ***p<0.001, ****p<0.0001; by Mann–Whitney U 2-tailed test.
Fig 5: KEGG pathway enrich map of the common response DEGs to RNase3 and RNase3-H15A treatment of THP1-derived macrophages. KEGG pathways enriched by a common up-regulated DEGs and b common down-regulated DEGs
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