EMBO/sd-character-level-ner huggingface dataset:
Pharmacologic inhibition of USP28 with AZ1 reduces tumour growth in an orthotopic model of lung SCC tumours.Figure 8Immunofluorescence (IF) staining against endogenous ∆Np63 in KP and KPL cell lines (blue: DAPI [staining of nuclei] and red/magenta: ∆Np63), Scale bar = 32µm. Schematic diagram of AZ1 treatment. After first 28 days without treatment, tumours were treated with an AZ1 dosage every 3 days until day 46. GFP Fluorescent images of lungs treated with either PBS/DMSO/0,1% Tween80 or indicated concentrations of AZ1. Tumour cells are positive for GFP (green arrows). n=3 Quantification of % tumour area (normalised to total lung area) in control (n=5), 125 mg/kg AZ1 (n=4) and 375 mg/kg AZ1 (n=4) treated animals. Representative staining of H&E and IHC for USP28 and ∆Np63 of SCC tumours from mice treated with PBS/DMSO/0,1% Tween80 or indicated concentrations of AZ1. Boxes indicate highlighted tumour areas. First line Scale bars = 500µm; Lower scale bars = 20µm. n=3   ∆Np63 staining intensity of lung tumours treated with PBS/DMSO/0,1%Tween80 or indicated concentrations of AZ1. nControl = 33712 cells ; nAZ1 125mg/kg = 7382 cells; nAZ1 375mg/kg = 4967 cells. Cells were analysed from three independent animals.   Schematic model
QKI knockout mice are resistant to hypothermia upon cold stimulus.Figure 7The rectal temperature of WT fl/fl and QKI KO fl/fl:AP2-Cre mice was monitored upon acute cold exposure (4 °C). (n = 10 mice, per group) H&E staining and UCP1 immunostaining of sections of ingWAT from WT fl/fl and QKI KO fl/fl:AP2-Cre mice at RT (22 °C) or following 72 h of cold exposure (4 °C). (Scale bar: 50 μm). The protein levels of UCP1 in ingWAT from WT fl/fl and QKI KO fl/fl:AP2-Cre mice at RT or following 72 h of cold exposure (4 °C), and quantified protein levels are shown in (D). (n=3 biological replicates, per group) Red Nile staining in BAT injected with Control or QKI knockdown AAV at RT (22 °C) or following 6 h and 72 h of cold exposure (4 °C). TG content in BAT injected with Control or QKI knockdown AAV at RT (22 °C) or following 6 h and 72 h of cold exposure (4 °C). The UCP1 protein level in BAT at RT or following 6 h and 72 h of cold exposure (4 °C) and the quantified protein levels. (n = 4 biological replicates, per group) The mRNA levels of genes related to energy consumption (PGC1α, UCP1 and Dio2). (n=4 biological replicates, per group)
Figure 1(A) Family pedigree. Variant segregation analysis of PSMC3. Electropherogram of a part of intron 10 of PSMC3 encompassing the identified variation (c.[1127+337A>G];[1127+337A>G], p.[(Ser376Arg15*)];[(Ser376Arg15*)]) in the affected individuals, their unaffected parents and siblings. The variation was found at the homozygous state in the affected individuals (II.2, II.4, II.7), at the heterozygous state in the parents (I.1, I.2, I.3, I.4, I.5, I.6) and was either at the heterozygous state (II.5) or absent in the unaffected siblings (II.1, II.3, II.6). (B) Face (up) and profile (down) photographs for patients II.4 (a: 8 yo, b: 16 yo), II.2 (c: 6 yo, d: 14 yo) and II.7 (e: 1 yo, f: 7 yo) over time. One can observe prominent supraciliay arches, synophris, sunken cheeks, short philtrum and retrusion in the malar region. (C) Sub cutaneous calcifications found only on knees (g: 9 yo and h: 16 yo) on elbows (i: 9 yo) of patient II.4. White hair were present only on the legs of the 3 patients as illustrated for patient II.4 (j: 16 yo). (D) Temporal bone CT-scan from patient II.7 (left column) and a control (right column) showing malformation of the semicircular canal. The left ear is shown on the upper panels while de right ear on the lower panels. (E) Amplification of the cDNA fragment between exons 9-10 and 11 of PSMC3 showing the abnormally spliced RNA fragment. One band at 180bp representing the normal allele is seen for the control and two bands for the individual II.4 (pathologic allele at 300bp). (F) Schematic representation for the incorporation of the 114bp intronic sequence resulting from the c.1127+337A>G deep intronic variation on the mRNA. Sanger sequencing of the fragment between exons 9-10 and 11 of the PSMC3 cDNA obtained from patient II.4 fibroblasts' RNA, showing the insertion of the 114bp cryptic exon. As a comparison, the schematic representation and sequence from a control individual are shown below.
Without pCtIP, NBS1 promotes the MR endonuclease independently of its FHA and BRCT domains.Figure 3Nuclease assays with MR and various NBS1 fragments (50 nM) on oligonucleotide-based 5'-end labeled dsDNA. The reaction buffer contained 60 mM NaCl and reactions were incubated for 2 h.   Quantitation of experiments such as shown in (A). Averages shown; n ≥ 3, error bars, SEM.
Figure 2A. Histograms show the luc activity obtained from zebrafish embryos microinjected simultaneously with puORFchop-luc, phRG-TK, and each indicated plasmid followed by analysis of luc activity at 96 hpf. Embryos microinjected with pCS2 vector during normal condition (non-stress; blank column) served as a control group, while the microinjected embryos treated with 40℃ at 72 hpf for 1 hr were the heat-shocked group (solid column). The relative luc activity of microinjected embryos shown on the right was normalized by the amount of RNA in the injected embryos shown on the left. The relative luc activity was represented by the fold increase of Fluc/Rluc ratio over that obtained from the control group (this was normalized to 1). The luc activity mediated by the huORFchop transcript was measured by dual-luciferase assay, and its corresponding huORFchop-luc transcript was measured by RT-qPCR. Values representing the non-stress and stress condition were calculated from three independent experiments and presented as mean ± S.D. (n=3). Student's -t test was used to determine significant differences between each group (**: P<0.005, ***: P <0.001). B. Histograms present the luc activity obtained from HEK 293T cells co-transfected with puORFchop-luc, phRG-TK, and each indicated plasmid and then treated with either DMSO (control group) or thapsigargin (TH; stress group), followed by analysis of luc activity. Cells transfected with pCS2-vector and kept at normal condition served as a control group. The relative luc activity of transfected cells shown on the right was normalized by the amount of mRNA in the transfected cells shown on the left. The relative luc activity was represented by the fold increase of Fluc/Rluc ratio over that obtained from pCS2-transfected control group (this was normalized to 1). The luc activity mediated by the huORFchop transcript was measured by Dual-Luciferase assay, and its corresponding huORFchop-luc transcript was measured by RT-qPCR. Values representing the non-stress and stress conditions were calculated from three independent experiments and presented as mean ± S.D. (n=3). Student's -t test was used to determine significant differences between each group (**: P<0.005, ***: P <0.001). C-E. Western blot analysis of proteins, as indicated, in (C) zebrafish embryos, (D) HEK 293T cells and (E) HeLa cells. GAPDH and α-tubulin served as internal controls. Protein levels relative to each internal control are presented below each lane.
NMR spectra of metabolite mixes.Figure 11D 1H-NMR spectra of a metabolite mix and the individual metabolites contained therein. Identification of single compound peaks from 1D 1H-NMR spectra of a metabolite mix. Compound detection is exemplified by showing sections of the 1D 1H-NMR spectra of ATP, IMP, proline (PRO), malate (MAL), shikimate (SKM) and methionine (MET).
Increased whole-body oxygen consumption and lipid utilization, and improved resistance to cold exposure in Cdk4-/- mice.Figure 1A-F Indirect calorimetry was performed using the Oxymax/CLAMS system in Cdk4+/+ (n=6) and Cdk4-/- (n=5) mice. Whole-body oxygen consumption rate (VO2) (A-B), energy expenditure (EE) (C-D) and respiratory exchange ratio (RER) (E-F) were measured at 24°C and during a cold challenge at 6°C during both the light (white rectangle) and dark (black rectangle) phases over a 2-day period. CalR was used to GLM-regression plot for each group corresponding to the association between energy balance and total body mass at 24°C (G) and the association between energy balance and total body mass at 6°C (H). The CalR interface displays each mouse as a dot, and the standard error of mean for each group in grey. The « mass effect » and « group effect » were analysed using a generalised linear model (GLM) using body weight as a covariate. The results of this analysis are shown in table (I) for Cdk4+/+ (n=6) and Cdk4-/- (n=5) mice. J-K Basal rectal temperature was measured at 24°C (J), and rectal temperature was monitored during acute cold exposure at 4°C for 6 hours (K) in Cdk4+/+ (n=10) and Cdk4-/- (n=8) mice.
Figure 5(A) Co-immunoprecipitation experiment in 12-day-old Col-0 pFLS2::FLS2-GFP seedlings. Protein extraction was performed 10 min after mock, 1 μM flg22 or 1 μM flg22 + 1 μM GLV2 treatment. IP was performed using GFP-TRAP agarose beads. Western blots for protein detection were probed with α-GFP or α-BAK1 antibodies. Data information: Similar results were obtained in 3 independent experiments. (B) Co-immunoprecipitation experiment upon co-expression of FLS2-HA with either CLV1-GFP or RGI3-GFP in N. benthamiana. IP was performed using GFP-TRAP agarose beads. Western blots for protein detection were probed with α-GFP or α-HA antibodies. Data information: Similar results were obtained in 3 independent experiments. (C) Co-immunoprecipitation experiment upon co-expression of FLS2-HA, BAK1-HA and RGI3-GFP in N. benthamiana. Protein extraction was performed 30 min after mock, 1 μM flg22 or 1 μM GLV2 treatment. IP was performed using GFP-TRAP agarose beads. Western blots for protein detection were probed with α-GFP or α-HA antibodies. Data information: Similar results were obtained in 3 independent experiments.
Metabolic intervention impacts Yap-driven growth phenotypes.Figure 6Effect of nucleoside (NS) cocktail treatment from 1-3 dpf on the incidence of cardiac edema in WT and yap-/- mutant larvae. Each point represents the percentage of affected embryos in each independent clutch. n>7, **p<0.01, two-sided Student's t-test; values represent the mean s.e.m Effect of WZB-117 (WZB, 10 μM) treatment from 3-5 dpf in WT and lf:Yap larvae on liver size as determined by fluorescence microscopy at 5 dpf in lf:GFP reporters. Scale bar: 200μm Quantitative analysis of the effect of WZB treatment from 3-5 dpf on liver size as determined by fluorescence microscopy. n>21, ****p<0.0001, two-sided Student's t-test; values represent the mean ± s.e.m Quantitative analysis of the effect of Trehalose (100 μM) treatment from 3-5 dpf on liver size as determined by fluorescence microscopy. n>70, ****p<0.0001, two-sided Student's t-test; values represent the mean ± s.e.m
Pyruvate transport activity of mitochondria containing MPCFERM or MPCOXMPCOX has higher transport activity than MPCFERM.Figure 4A MPCOX has higher transport activity than MPCFERM. The uptake of 14C‐labeled pyruvate into intact mitochondria was measured in vitro. Mitochondria had been isolated from cells grown in glycerol‐containing medium and expressing no subunit (vectors), MPCFERM, MPCOX, Mpc2, or Mpc3. Imported pyruvate was quantified by re‐isolation of mitochondria and subsequent scintillation counting after 1, 2, or 5 min of incubation with [14C]‐pyruvate.B Imported [14C]‐pyruvate as in (A) after 5‐min incubation. The difference between MPCOX and MPCFERM (**P = 0.0037) was significant (unpaired t‐test). C Pyruvate dehydrogenase activity was measured in lysates of mitochondria expressing no subunit (vectors), MPCFERM, or MPCOX.
Figure 3(A) Cell viability (TO-PRO-3 FACS staining) of GT1-7 neuronal cells transfected for 24 hours with either wild type or indicated mutant constructs containing either 80 G4C2 repeats or 100 C4G2 repeats embedded in sense or antisense C9ORF72 fused to the GFP in the GA, PG or GR frame. (B) Immunoblotting against the GFP, endogenous C9ORF72 or the GAPDH of proteins extracted from Neuro2A cells transfected for 24 hours with 80 G4C2 repeats embedded in the human sense C9ORF72 sequence fused to the GFP in the GA frame and with either a control siRNA or a siRNA targeting C9orf72 mRNA. (C) Immunoblotting against the HA tag, endogenous C9ORF72 or GAPDH of proteins extracted from Neuro2A cells transfected for 24 hours with 100 C4G2 repeats embedded in the human antisense C9ORF72 sequence fused to a HA tag in the PG frame and with either a control siRNA or a siRNA targeting C9orf72 mRNA or treated with Bafilomycin A1 for 15 hours. (D) Immunoblotting against the HA tag, endogenous C9ORF72 or GAPDH of proteins extracted from Neuro2A cells transfected for 24 hours with 80 G4C2 repeats embedded in the human sense C9ORF72 sequence fused to a HA tag in the GR frame and with either a control siRNA or a siRNA targeting C9orf72 mRNA or treated with Bafilomycin A1 for 15 hours. (E) Cell viability (TO-PRO-3 FACS staining) of GT1-7 neuronal cells co-transfected for 24 hours with either a control siRNA or a siRNA targeting C9orf72 mRNA and wild-type or mutants constructs containing either 80 G4C2 repeats or 100 C4G2 repeats embedded in sense or antisense C9ORF72 fused to the GFP in the GA, PG or GR frame.
Figure 7Plasma metabolomic changes revealed a trajectory in COVID-19 severity, from healthy control (n=12), mild (n=29), to severe (n=17). Changes in the concentration of plasma metabolites are associated with COVID-19 severity. The discharge group consist of all patients (mild and severe) that were recovered and discharged. L1, low-density lipoprotein subclass-1 (LDL1); VL, very low- density lipoprotein (VLDL); L5, LDL5; L6, LDL6; H2: high-density lipoprotein subclass-2 (HDL2); H3: HDL3; H4: HDL4. COVID-19 severity is associated with significant changes in lipoprotein subclasses including high-density lipoprotein subclass-1 (HDL1), HDL4, low-density lipoprotein subclasses (LDL1, LDL4, LDL5), very low-density lipoprotein subclass-5 (VLDL5) and their compositional components (ApoA1, triglycerides, cholesterol). TG: triglycerides; FC: free cholesterol; CE: cholesteryl esters; CH: total cholesterol (i.e., FC + CE); PL: total phospholipids; A1: ApoA1; A2: ApoA2; L1TG: TG in LDL1; L1TG%: percentages of L1TG in total lipids of LDL1; L1%: percentage of LDL1 in all LDL; L-TG%: percentages of L-TG(TG in LDL) in total lipids of LDL; V5FC%, V5CE%: percentages of V5FC(FC in VLDL5) and V5CE(CE in VLDL5) in total lipids of VLDL5; L5CE%, L5CH%: percentages of L5CE(CE in LDL5) and L5CH(CH in LDL5) in total lipids of LDL5; H1FC%: percentages of H1FC (FC in HDL1) in total lipids of HDL1; H-A2: ApoA2 in both HDL and nascent HDL; H4A1, H4A2, H4CE, H4CH, H4FC, H4PL: ApoA1, ApoA2, CE, CH, FC and PL in HDL4; Plasma levels of key enzymes and proteins directly involving lipoprotein metabolism are indicators for COVID-19 severity. Data were represented as means ± SD and differences between groups were estimated using a Student's t test. * p < 0.05; ** p < 0.01; *** p < 0.001. Control, n=12; mild, n=29; severe, n=17; discharge, n=16; sLDLR: soluble low-density lipoprotein receptor; LCAT: lecithin-cholesterol acyltransferase; CEPT: cholesteryl-ester transfer protein. COVID-19 caused dysregulation in lipoprotein metabolism, glycolysis and TCA cycle. The three boxes from left to right are control, mild and severe, in which gray means normal, blue means decrease, red means increase. CS: Citrate synthase; IDH: Isocitrate dehydrogenase; ACO2: Aconitase; OGDH: α-ketoglutarate dehydrogenase; DLD: Dihydrolipoyl dehydrogenase; SDH: Succinic dehydrogenase; MDH: Malate dehydrogenase; PDH: Pyruvate dehydrogenase; PDK: Pyruvate dehydrogenase kinase; ACLY: ATP citrate lyase; ACAC: Acetyl coenzyme A carboxylase; FASN: Fatty acid synthetase; LDH: Lactate dehydrogenase.
Fig.Figure 3A. Superposition of MID-PIWI lobes from seed-only (gray) and seed plus supplementary-paired (colored) structures shows only the PIWI Loop changes substantially between upon supplementary interactions (RNAs not shown for clarity). B. Superposition of N-PAZ lobe reveals minor twists in N and PAZ domains relative to L1, but overall structures are very similar between seed-only and seed plus supplementary-paired structures. C. Superposition of entire Ago2 structures reveals major differences are restricted to rigid body movement of the N-PAZ lobe relative to the MID-PIWI lobe. Movement centers around the β1- β19 hinge. D. Superposition of seed chambers in the seed-only paired (gray/semi-transparent) and seed plus supplementary-paired (colored) structures. Helix-7 (α7) contacts miRNA and target in both structures despite conformational shifts to accommodate opening of the supplementary chamber.
Figure 5(A) Transwell assay was performed to evaluate the invasion abilities of HCT116 cells after transfection of IDH1 K224R or knockout of IDH1. Quantification was performed by counting the stained cells that invaded to the lower chamber under a light microscopy. Data information: All results were expressed as mean ± SD of three independent experiments (n ≥ 3 per experimental condition). For A statistical significance was assessed with a one-way ANOVA with Newman-Keuls post hoc test. *P<0.05 and **P<0.01. (B) Three-dimension imaging analysis was to assessed velocity of cell movement. Data information: All results were expressed as mean ± SD of three independent experiments (n ≥ 3 per experimental condition). For B, statistical significance was assessed with a one-way ANOVA with Newman-Keuls post hoc test. *P<0.05 and **P<0.01. (C) Cell migration ability was evaluated by wound healing assay in HCT116 cells. Quantification was performed by measuring the smallest clearance distance of the wound. Data information: All results were expressed as mean ± SD of three independent experiments (n ≥ 3 per experimental condition). For figure C, statistical significance was assessed with a two-way ANOVA followed by Tukey's post hoc test. *P<0.05 and **P<0.01. (D) Colony formation ability after deacetylation of IDH1 K224 or knockout of IDH1. Data information: All results were expressed as mean ± SD of three independent experiments (n ≥ 3 per experimental condition). For statistical significance was assessed with a one-way ANOVA with Newman-Keuls post hoc test. *P<0.05 and **P<0.01. (E) Cell cycle distribution was assessed flow cytometrically after treatment with IDH1 K224R or knockout of IDH1. Data information: All results were expressed as mean ± SD of three independent experiments (n ≥ 3 per experimental condition). For E, statistical significance was assessed with a one-way ANOVA with Newman-Keuls post hoc test. *P<0.05 and **P<0.01.
Reduced interaction between Beclin 1, TAB and TAB3 in conditions of autophagy induction.Figure 2(A, B) Inhibition of autophagy by dominant‐negative (DN) TAK1. HeLa cells were co‐transfected with a GFP-LC3‐encoding construct plus pcDNA3.1 (empty vector), or plasmids for the expression of WT TAK1 (TAK1WT) or the DN TAK1K63W mutant. One day later, cells were either left untreated (control) or driven into autophagy by starvation or by the administration of 1 μM rapamycin or 30 μM pifithrin α (PFTα), followed by immunoblotting for the detection of TAK1 and endogenous LC3 (A) or immunofluorescence microscopy for the quantification of cells with cytosolic GFP-LC3 puncta (GFP-LC3VAC cells) (B) (mean values±s.d., n=3; *P0.01 versus control cells). GAPDH levels were monitored to ensure equal loading. (C, D) Inhibition of autophagy by knockdown of VPS34, Beclin 1 (BCN1) and TAK1. siRNAs that effectively deplete VPS34, BCN1 and TAK1 were co‐transfected with a GFP-LC3‐encoding plasmid in HeLa cells. Autophagy was then induced as in (A) and the frequency of GFP-LC3VAC cells (mean values±s.d., n=3; *P0.01 versus control cells) was determined. (E, F) The same setting shown in (C, D) was performed with U2OS cells and FYVE-RFP (mean values±s.d., n=3; *P0.01, **P0.001 versus control cells).
Figure 6(A) Immunoprecipitation/mmunoblot of E3 ubiquitin ligases by PERK and the binding to mutant LRRK2. HEK293 cells were transfected with PERK and either MARCH5, MULAN or Parkin, LRRK2, LRRK2(D1994A) or LRRK2(S1292D). Cell lysates were immunoprecipitated with antibody against Myc or V5, and precipitates were immunoblotted with antibody indicated the right. (B) In vitro kinase assay for auto-phosphorylated LRRK2 using isolated LRRK2 mutants and [γ-32P]ATP with or without LRRK2-IN-1 (1 μM). Mutant LRRK2 precipitated with antibody against V5 was subjected to SDS/PAGE. Blots were with antibody against V5 or phosphoserine. [γ-32P]ATP-incorporated LRRK2 visualized by autoradiography. (C) Binding assays to detect interactions between phosphomimetic LRRK2(S1292D) or phosphorylation-defective LRRK2(S1292A) and E3 ubiquitin ligases. HEK293 cells were transfected with LRRK2 mutants and E3 ubiquitin ligases lysates were immunoprecipitated with antibody against Myc or V5 epitope. Precipitated proteins were subjected to SDS/PAGE, for immunoblotwith antibody against V5 or Myc. (D) Immunoprecipitation/mmunoblot of E3 ubiquitin ligases by PERK-ΔN in the presence of LRRK2(S1292A) or LRRK2(S1292D). HEK293 cells were transfected with MARCH5, MULAN, Parkin, and PERK-ΔN LRRK2(S1292A) or LRRK2(S1292D). Cell lysates were immunoprecipitated with antibody against Myc, and precipitates were immunoblotted with antibody indicated the right.
VHHmASC ameliorates MSU gouty inflammation.Figure 6(A) Schematic representation of the experimental setting used for the MSU-gout model. Mice were injected i.a with 100 µg of monosodium urate (MSU) crystals into the knee. After 3 h, mice were treated intraperitonially (i.p.) with VHHmASC, VHH NP-1 as unrelated nanobody (both 5 mg kg-1), or vehicle (PBS). (B) Mechanical allodynia threshold and edema were evaluated at 3 and 6 hour post-MSU challenge. Error bars represent SEM from biological replicates: t0, n=3 for all groups; t3 and t6: PBS + VHH NP-1 and PBS + VHHmASC, n=3 (Mechanical threshold) or n=4 (Edema); MSU + Vehicle, n=4; MSU + VHH NP-1, n=7; MSU + VHHmASC, n=7. (C) Flow cytometric assessment of infiltrating total leukocytes (CD45+) and granulocytes (CD45+ Ly6G+ Ly6C-) recovered in the synovial fluid of the knee joints of mice treated as in (A). Data in (C) is displayed as floating bars with the max/min values and mean (thicker band). Biological replicates are: PBS + VHH NP-1, n=4; PBS + VHHmASC, n=4; MSU + Vehicle, n=4; MSU + VHH NP-1, n=7; MSU + VHHmASC, n=7. (D) ELISA of IL-1β, TNFα and IL-6 in tissue homogenates of knee joints of mice treated as in (A). Data in (C) is displayed as floating bars with the max/min values and mean (thicker band). Biological replicates are PBS + VHH NP-1, n=4; PBS + VHHmASC, n=4; MSU + Vehicle, n=4; MSU + VHH NP-1, n=7; MSU + VHHmASC, n=7.
Figure 10A The developmental upregulation of Atossa in macrophages increases mRNA levels of the nucleolar protein Pths and the metabolic enzymes GR/HPR and LKR/SDH. Metabolic pathways downstream of GR/HPR and LKR/SDH are known to produce metabolites that feed into glycolysis and the TCA cycle to produce ATP. Pths enhances the translational efficiency of a subset of mRNAs, including those encoding mitochondrial ETC components. Macrophages with elevated mitochondrial OxPhos can meet their emerging energy demands for tissue invasion. B However, the absence of Atos leads to reduced levels of GR/HPR, LKR/SDH and Porthos. This decreases the OxPhos-generated ATP supply leading to defective tissue infiltration of the pioneering macrophages.
TLRs activation restores LC3-II expression and inhibits the growth of Mfa1+Pg within human MoDCs.Fig 8A) Flow cytometry of CD83 on MoDCs after incubation of TLR4 ligand (E. coli LPS) and TLR1 and 2 ligand (Pam3csk4) for 4 hour. B) Immuno-fluorescence images of LC3-II (red) within MoDCs after incubation with TLR4 and TLR1&amp;amp;2 ligands (E. coli LPS and Pam3csk4) C) The plot represents the means ±standard deviation of CFU within MoDCs harvested from three healthy individuals after 24 hours (** p<0.001).