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antibodies against c3  (Cedarlane)


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    Cedarlane antibodies against c3
    Complement is fixed on KEL RBCs in-vivo and in-vitro in response to polyclonal anti-KEL (KELIg). (A) General in-vivo experimental design: recipients were treated with or without KELIg and transfused with DiO labeled KEL RBCs. (B) <t>C3,</t> C4, and Factor B were measured on recovered DiO positive KEL RBCs 1-hour post-transfusion; black filled histogram shows condition without KELIg; grey shaded histogram shows condition with KELIg. (C) In-vitro experiments were completed with KELIg incubated with KEL RBCs in the presence (darkest histogram) or absence (lightest histogram) of serum; an additional condition included saline incubated with KEL RBCs in the presence of serum (medium grey histogram). (D) Additional in-vitro conditions included KELIg incubated with KEL RBCs in the presence of serum (darkest histogram), in the presence of serum with EGTA-Mg (lightest histogram) or serum with EDTA (medium grey histogram). These data are representative of 3 independent experiments; p < 0.05 for C3 detection on RBCs in the presence or absence of KELIg.
    Antibodies Against C3, supplied by Cedarlane, used in various techniques. Bioz Stars score: 92/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/mouse+complement+c3/Anti-Mouse+Complement+Component+C3%2C+Biotin+(Clone+RmC11H9)+(rat+IgG2a)/pmc08270673-41-14-18
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    antibodies against c3 - by Bioz Stars, 2026-09
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    Images

    1) Product Images from "Complement Plays a Critical Role in Inflammation-Induced Immunoprophylaxis Failure in Mice"

    Article Title: Complement Plays a Critical Role in Inflammation-Induced Immunoprophylaxis Failure in Mice

    Journal: Frontiers in Immunology

    doi: 10.3389/fimmu.2021.704072

    Complement is fixed on KEL RBCs in-vivo and in-vitro in response to polyclonal anti-KEL (KELIg). (A) General in-vivo experimental design: recipients were treated with or without KELIg and transfused with DiO labeled KEL RBCs. (B) C3, C4, and Factor B were measured on recovered DiO positive KEL RBCs 1-hour post-transfusion; black filled histogram shows condition without KELIg; grey shaded histogram shows condition with KELIg. (C) In-vitro experiments were completed with KELIg incubated with KEL RBCs in the presence (darkest histogram) or absence (lightest histogram) of serum; an additional condition included saline incubated with KEL RBCs in the presence of serum (medium grey histogram). (D) Additional in-vitro conditions included KELIg incubated with KEL RBCs in the presence of serum (darkest histogram), in the presence of serum with EGTA-Mg (lightest histogram) or serum with EDTA (medium grey histogram). These data are representative of 3 independent experiments; p < 0.05 for C3 detection on RBCs in the presence or absence of KELIg.
    Figure Legend Snippet: Complement is fixed on KEL RBCs in-vivo and in-vitro in response to polyclonal anti-KEL (KELIg). (A) General in-vivo experimental design: recipients were treated with or without KELIg and transfused with DiO labeled KEL RBCs. (B) C3, C4, and Factor B were measured on recovered DiO positive KEL RBCs 1-hour post-transfusion; black filled histogram shows condition without KELIg; grey shaded histogram shows condition with KELIg. (C) In-vitro experiments were completed with KELIg incubated with KEL RBCs in the presence (darkest histogram) or absence (lightest histogram) of serum; an additional condition included saline incubated with KEL RBCs in the presence of serum (medium grey histogram). (D) Additional in-vitro conditions included KELIg incubated with KEL RBCs in the presence of serum (darkest histogram), in the presence of serum with EGTA-Mg (lightest histogram) or serum with EDTA (medium grey histogram). These data are representative of 3 independent experiments; p < 0.05 for C3 detection on RBCs in the presence or absence of KELIg.

    Techniques Used: In Vivo, In Vitro, Labeling, Incubation, Saline

    Recipient C3 and C1q contribute to KELIg immunoprophylaxis failure in the setting of poly (I:C). (A) General in-vivo experimental design: recipients were infused with KELIg and transfused the following day in the absence or presence of poly (I:C) treatment, with anti-KEL responses evaluated longitudinally. (B) Anti-KEL IgG responses in wild type compared with C3 -/- recipients transfused in the absence of poly (I:C). (C) Anti-KEL IgG responses in wild type compared with C3 -/- recipients transfused in the presence of poly (I:C). (D) Anti-KEL IgG responses in wild type compared with C1q -/- recipients transfused in the presence of poly (I:C). (E) Baseline impact of recipient treatment with poly (I:C) on alloimmune responses to KEL RBCs in the absence of KELIg. These data are representative of 2-3 independent experiments, with 3-5 mice/group/experiment; error bars indicate standard deviation between individual mice. *p < 0.05 (C, D) d14,21,28, and all comparisons for (E) .
    Figure Legend Snippet: Recipient C3 and C1q contribute to KELIg immunoprophylaxis failure in the setting of poly (I:C). (A) General in-vivo experimental design: recipients were infused with KELIg and transfused the following day in the absence or presence of poly (I:C) treatment, with anti-KEL responses evaluated longitudinally. (B) Anti-KEL IgG responses in wild type compared with C3 -/- recipients transfused in the absence of poly (I:C). (C) Anti-KEL IgG responses in wild type compared with C3 -/- recipients transfused in the presence of poly (I:C). (D) Anti-KEL IgG responses in wild type compared with C1q -/- recipients transfused in the presence of poly (I:C). (E) Baseline impact of recipient treatment with poly (I:C) on alloimmune responses to KEL RBCs in the absence of KELIg. These data are representative of 2-3 independent experiments, with 3-5 mice/group/experiment; error bars indicate standard deviation between individual mice. *p < 0.05 (C, D) d14,21,28, and all comparisons for (E) .

    Techniques Used: In Vivo, Standard Deviation

    Recipient complement, KEL RBC clearance, and KEL antigen expression. KEL RBCs were labeled with DiO and mixed with wild type RBCs labeled with DiI; this mixture was transfused into recipients that had been infused with KELIg and treated with poly (I:C). (A) shows wild type compared with C3 -/- recipients; (B) shows wild type compared with C1q -/- recipients. Recovered DiO labeled RBCs were then evaluated for KEL glycoprotein expression by flow cytometry, after incubation with KELIg and fluorescently conjugated anti-mouse IgG; (C) shows wild type recipients compared with C3 -/- recipients; (D) shows wild type recipients compared with C1q -/- recipients. These data are representative of 2-3 independent experiments with 3 mice/group/experiment; error bars indicate standard deviation between mice. *p < 0.05 for all comparisons in (C) and p = ns, not significant for all comparisons in (D) .
    Figure Legend Snippet: Recipient complement, KEL RBC clearance, and KEL antigen expression. KEL RBCs were labeled with DiO and mixed with wild type RBCs labeled with DiI; this mixture was transfused into recipients that had been infused with KELIg and treated with poly (I:C). (A) shows wild type compared with C3 -/- recipients; (B) shows wild type compared with C1q -/- recipients. Recovered DiO labeled RBCs were then evaluated for KEL glycoprotein expression by flow cytometry, after incubation with KELIg and fluorescently conjugated anti-mouse IgG; (C) shows wild type recipients compared with C3 -/- recipients; (D) shows wild type recipients compared with C1q -/- recipients. These data are representative of 2-3 independent experiments with 3 mice/group/experiment; error bars indicate standard deviation between mice. *p < 0.05 for all comparisons in (C) and p = ns, not significant for all comparisons in (D) .

    Techniques Used: Expressing, Labeling, Flow Cytometry, Incubation, Standard Deviation

    Poly (I:C) and KELIg immunoprophylaxis result in increased transfused KEL RBC consumption by splenic inflammatory monocytes in wild type compared with C3 -/- mice. DiO labeled KEL RBCs were transfused to wild type or C3 -/- mice treated with KELIg in the presence or absence of poly (I:C) and splenic cell subsets were evaluated at 1 and 16 hours post-transfusion (A, B) . (C) Representative histograms for DiO RBC fluorescence patterns of inflammatory monocytes at 16 hours post-transfusion, after first excluding TER119 positive RBCs on the exterior of the splenic cells; black open histogram is KELIg in wild type, dotted open histogram is KELIg and PIC in wild type; white shaded histogram is KELIg in C3 -/- and dotted shaded histogram is KELIg and PIC in C3 -/- . DiO mean fluorescence intensity (MFI) of the splenic cell subsets was evaluated at 1 hour (D) and 16 hours (E) post-transfusion. These data are representative of 2-3 independent experiments with 3 mice/group/experiment; error bars indicate standard deviation between mice.
    Figure Legend Snippet: Poly (I:C) and KELIg immunoprophylaxis result in increased transfused KEL RBC consumption by splenic inflammatory monocytes in wild type compared with C3 -/- mice. DiO labeled KEL RBCs were transfused to wild type or C3 -/- mice treated with KELIg in the presence or absence of poly (I:C) and splenic cell subsets were evaluated at 1 and 16 hours post-transfusion (A, B) . (C) Representative histograms for DiO RBC fluorescence patterns of inflammatory monocytes at 16 hours post-transfusion, after first excluding TER119 positive RBCs on the exterior of the splenic cells; black open histogram is KELIg in wild type, dotted open histogram is KELIg and PIC in wild type; white shaded histogram is KELIg in C3 -/- and dotted shaded histogram is KELIg and PIC in C3 -/- . DiO mean fluorescence intensity (MFI) of the splenic cell subsets was evaluated at 1 hour (D) and 16 hours (E) post-transfusion. These data are representative of 2-3 independent experiments with 3 mice/group/experiment; error bars indicate standard deviation between mice.

    Techniques Used: Labeling, Fluorescence, Standard Deviation

    Complement-fixed KEL RBCs bind in-vitro to wild type donor derived B-cells but not to CR1/2 -/- B-cells. DiO labeled KEL RBCs were incubated with KELIg in the presence of sera, followed by incubation with peripheral blood derived WBCs from donor mice. (A) In wells using WBCs from wild type donor mice, CD19+B220+ B-cells cells were separated by DiO positivity and then by C3 positivity. The CD19+B220+ cells were next separated by their CD23 and CD21/35 expression, with the cells highest for CD23 and CD21/35 gated in the larger gate and those less strongly positive for CD23 and CD21/35 gated in the smaller gate; the DiO positive and negative populations were then evaluated for their C3 positivity. Shaded histograms are the DiO positive population, open histograms are the DiO negative population. (B) In wells using WBCs from CR1/2 -/- mice, CD19+B220+ B-cells cells were separated by DiO positivity and then by C3 positivity. Shaded histograms are the DiO positive population, open histograms are the DiO negative population. These data are representative of more than 3 independent experiments, with 2 involving CD23 and CD21/35 staining.
    Figure Legend Snippet: Complement-fixed KEL RBCs bind in-vitro to wild type donor derived B-cells but not to CR1/2 -/- B-cells. DiO labeled KEL RBCs were incubated with KELIg in the presence of sera, followed by incubation with peripheral blood derived WBCs from donor mice. (A) In wells using WBCs from wild type donor mice, CD19+B220+ B-cells cells were separated by DiO positivity and then by C3 positivity. The CD19+B220+ cells were next separated by their CD23 and CD21/35 expression, with the cells highest for CD23 and CD21/35 gated in the larger gate and those less strongly positive for CD23 and CD21/35 gated in the smaller gate; the DiO positive and negative populations were then evaluated for their C3 positivity. Shaded histograms are the DiO positive population, open histograms are the DiO negative population. (B) In wells using WBCs from CR1/2 -/- mice, CD19+B220+ B-cells cells were separated by DiO positivity and then by C3 positivity. Shaded histograms are the DiO positive population, open histograms are the DiO negative population. These data are representative of more than 3 independent experiments, with 2 involving CD23 and CD21/35 staining.

    Techniques Used: In Vitro, Derivative Assay, Labeling, Incubation, Expressing, Staining

    CR1/2 are required for KELIg immunoprophylaxis failure in the setting of poly (I:C). (A) KEL RBCs were transfused into wild type recipients or recipients lacking CR1/2, in the presence or absence of poly (I:C). (B) RBCs were labeled with DiO and mixed with wild type RBCs labeled with DiI; this mixture was transfused into wild type or CR1/2 -/- recipients that had been infused with KELIg and treated with poly (I:C). Recovered DiO positive KEL RBCs were evaluated for (C) KEL glycoprotein expression, and (D) bound complement C3. (E) Wild type or CR1/2 -/- recipients were infused with KELIg and transfused the following day in the absence or presence of poly (I:C), with anti-KEL responses evaluated longitudinally. *p < 0.05 for d14, 21 and 28 of (A) between CR1/2 -/- mice treated with or without poly (I:C); p < 0.05 for 10 min and 1-hour timepoints in (C) ; p < 0.05 for d14, 21, and 28 in (E) . These data are representative of 2-3 independent experiments with 3 mice/group/experiment; error bars indicate standard deviation between mice. ns, not significant.
    Figure Legend Snippet: CR1/2 are required for KELIg immunoprophylaxis failure in the setting of poly (I:C). (A) KEL RBCs were transfused into wild type recipients or recipients lacking CR1/2, in the presence or absence of poly (I:C). (B) RBCs were labeled with DiO and mixed with wild type RBCs labeled with DiI; this mixture was transfused into wild type or CR1/2 -/- recipients that had been infused with KELIg and treated with poly (I:C). Recovered DiO positive KEL RBCs were evaluated for (C) KEL glycoprotein expression, and (D) bound complement C3. (E) Wild type or CR1/2 -/- recipients were infused with KELIg and transfused the following day in the absence or presence of poly (I:C), with anti-KEL responses evaluated longitudinally. *p < 0.05 for d14, 21 and 28 of (A) between CR1/2 -/- mice treated with or without poly (I:C); p < 0.05 for 10 min and 1-hour timepoints in (C) ; p < 0.05 for d14, 21, and 28 in (E) . These data are representative of 2-3 independent experiments with 3 mice/group/experiment; error bars indicate standard deviation between mice. ns, not significant.

    Techniques Used: Labeling, Expressing, Standard Deviation



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    Fitc Anti Mouse C3b, supplied by Cedarlane, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    anti mouse complement c3 antibody  (Valiant Co Ltd)
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    Valiant Co Ltd anti mouse complement c3 antibody
    The requirement of the <t>complement</t> system for Ficolin-A-based immunity. A. The contribution of <t>C3</t> to hepatic clearance of Spn-19F . Bacteria in the blood (left) and liver/spleen (right) of C3 -/- mice were quantified post i.v. infection with 10 6 (left) or 10 7 CFU (right). n = 3. B. The role of C3 receptors to hepatic clearance of Spn-19F . CRIg -/- , CR3 -/- and CRIg / CR3 -/- mice were infected with 10 6 (left) or 10 7 CFU (right) to quantify bacteria as in (A). n = 3. C. The role of the lectin pathway in hepatic clearance of Spn-19F . Masp1 -/- and Masp2 -/- mice were infected with 10 6 (left) or 10 7 CFU (right) to quantify bacteria as in (A). n = 3. D. Visualization of bacterial capture by KCs of complement-deficient mice. The liver sinusoids of C3 -/- , CRIg / CR3 -/- and Masp2 -/- mice were imaged by intravital microscopy as in 2D. n = 2. E. Complement-dependent bacterial capture by KCs in vitro . Primary mouse KCs were incubated with Spn- 19F in the presence of 10% serum for 30 min. Spn- 14 was used as a negative control. KC-bound bacteria are presented as the percentage of total bacteria. MOI = 1; n = 3-6. F. The importance of the complement system in the protection against Spn- 19F. Various complement-deficient mice were i.v. infected with 10 6 CFU of Spn- 19F and the survival is presented. n = 5. G. The model for the FCN-A-triggered complement-dependent and -independent pathways for bacterial capture by liver macrophages. FCN-A activates C3 on bacterial surface upon binding to the capsule through the lectin pathway. The representative data are presented as mean ± SD, and the statistical differences were determined by Two-way ANOVA with Tukey’s multiple comparisons test (A-C), multiple t tests (D and E) and log-rank test (F). **, P < 0.01; ****, P < 0.0001; ns, no significant difference.
    Anti Mouse Complement C3 Antibody, supplied by Valiant Co Ltd, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Schematic illustration of in vivo tumor immunotherapy enhanced by mRNA/HNPs through intravenous injection. H18 lipid, DOPE, cholesterol, DMG-PEG 2000 and mRNA were mixed to form mRNA/H 18 NPs with the special multilamellar concentric nanostructures. Following intravenous administration, mRNA/H 18 NPs demonstrated preferential adsorption of complement C3 proteins to form a characteristic protein corona, resulting in specific mRNA transfection in the spleen, especially in splenic dendritic cells. When encapsulating tumor antigen-encoding mRNA, the mRNA/H 18 NPs achieved precise transfection of the antigen mRNA in splenic dendritic cells. This targeted delivery stimulated dendritic cell maturation and subsequent antigen presentation, initiating robust T cell priming. The activated antigen-specific cytotoxic T lymphocytes then infiltrated into tumor tissues, ultimately inducing tumor cell elimination.

    Journal: Bioactive Materials

    Article Title: Splenic dendritic cell-targeting mRNA transfection of H-type ionizable lipid-based LNPs for enhancing tumor immunotherapy

    doi: 10.1016/j.bioactmat.2026.02.018

    Figure Lengend Snippet: Schematic illustration of in vivo tumor immunotherapy enhanced by mRNA/HNPs through intravenous injection. H18 lipid, DOPE, cholesterol, DMG-PEG 2000 and mRNA were mixed to form mRNA/H 18 NPs with the special multilamellar concentric nanostructures. Following intravenous administration, mRNA/H 18 NPs demonstrated preferential adsorption of complement C3 proteins to form a characteristic protein corona, resulting in specific mRNA transfection in the spleen, especially in splenic dendritic cells. When encapsulating tumor antigen-encoding mRNA, the mRNA/H 18 NPs achieved precise transfection of the antigen mRNA in splenic dendritic cells. This targeted delivery stimulated dendritic cell maturation and subsequent antigen presentation, initiating robust T cell priming. The activated antigen-specific cytotoxic T lymphocytes then infiltrated into tumor tissues, ultimately inducing tumor cell elimination.

    Article Snippet: Mouse Complement C3 was purchased from MedChemExpress.

    Techniques: In Vivo, Injection, Adsorption, Transfection, Immunopeptidomics

    In vivo splenic DC-specific transfection of mRNA/H 18 NPs and in vitro protein corona analysis of mRNA/H 18 NPs. (A) EGFP protein expression in splenic cell subsets of C57BL/6J mice 24 h post intravenous injection of different formulations. (B) The top 5 most abundant plasma proteins adsorbed on mRNA/H 18 NPs (C3: Complement C3; Ighm: Immunoglobulin heavy constant mu; Hbat1: Alpha-globin; Itih4: Inter alpha-trypsin inhibitor, heavy chain 4; Cnn2: Calponin). (C) Heatmap plot of major proteins in the protein corona adsorbed on mRNA/MC3-LNPs and mRNA/H 18 NPs. PBS group was used as a negative control. (D) Quantification of major adsorbed protein categories of different formulations. (E) Complement C3 abundance in protein corona adsorbed on mRNA/MC3-LNPs and mRNA/H 18 NPs. (F) Bioluminescence images of major organs and (G) Quantification of total bioluminescence flux in the spleen from C57BL/6J mice 6 h after intravenous injection of mLuc/H 18 NPs (mLuc dose of 0.25 mg kg −1 ). Mice were pre-treated with cobra venom factor (CVF) or PBS. (H) Fluorescence quantification of Cy5 mRNA delivered by uncoated or complement C3-coated Cy5-mRNA/H 18 NPs in BMDCs. BMDCs were pre-incubated with anti-CD11b (CR3) or anti-IgG blocking antibody. (I) Bioluminescence intensity of luciferase protein translated from mRNA delivered by uncoated or complement C3-coated mLuc/H 18 NPs in BMDCs. BMDCs were pre-incubated with anti-CD11b (CR3) or anti-IgG blocking antibody. Data were shown as mean ± SD (n = 3).

    Journal: Bioactive Materials

    Article Title: Splenic dendritic cell-targeting mRNA transfection of H-type ionizable lipid-based LNPs for enhancing tumor immunotherapy

    doi: 10.1016/j.bioactmat.2026.02.018

    Figure Lengend Snippet: In vivo splenic DC-specific transfection of mRNA/H 18 NPs and in vitro protein corona analysis of mRNA/H 18 NPs. (A) EGFP protein expression in splenic cell subsets of C57BL/6J mice 24 h post intravenous injection of different formulations. (B) The top 5 most abundant plasma proteins adsorbed on mRNA/H 18 NPs (C3: Complement C3; Ighm: Immunoglobulin heavy constant mu; Hbat1: Alpha-globin; Itih4: Inter alpha-trypsin inhibitor, heavy chain 4; Cnn2: Calponin). (C) Heatmap plot of major proteins in the protein corona adsorbed on mRNA/MC3-LNPs and mRNA/H 18 NPs. PBS group was used as a negative control. (D) Quantification of major adsorbed protein categories of different formulations. (E) Complement C3 abundance in protein corona adsorbed on mRNA/MC3-LNPs and mRNA/H 18 NPs. (F) Bioluminescence images of major organs and (G) Quantification of total bioluminescence flux in the spleen from C57BL/6J mice 6 h after intravenous injection of mLuc/H 18 NPs (mLuc dose of 0.25 mg kg −1 ). Mice were pre-treated with cobra venom factor (CVF) or PBS. (H) Fluorescence quantification of Cy5 mRNA delivered by uncoated or complement C3-coated Cy5-mRNA/H 18 NPs in BMDCs. BMDCs were pre-incubated with anti-CD11b (CR3) or anti-IgG blocking antibody. (I) Bioluminescence intensity of luciferase protein translated from mRNA delivered by uncoated or complement C3-coated mLuc/H 18 NPs in BMDCs. BMDCs were pre-incubated with anti-CD11b (CR3) or anti-IgG blocking antibody. Data were shown as mean ± SD (n = 3).

    Article Snippet: Mouse Complement C3 was purchased from MedChemExpress.

    Techniques: In Vivo, Transfection, In Vitro, Expressing, Injection, Clinical Proteomics, Negative Control, Combined Bisulfite Restriction Analysis Assay, Fluorescence, Incubation, Blocking Assay, Luciferase

    (A) The impact of OMVs on germicidal activity of serum against YeO3‐c bacteria. The influence of OMVs‐associated with: LPS polysaccharide chain length (a) and pYV‐coded factors (b). Data from one of at least two experiments with the use of separately prepared culture supernatants with similar results are presented. 1 sterile cell culture supernatants (secreted by bacteria grown to OD 600 = 0.6) were used as a source of OMVs; 2 expression at 37°C only; 3 NHS inactivated 30 min at 56°C. (B) Y. enterocolitica O:3 OMV‐induced complement activation in the presence of calcium and magnesium chelators. ELISA plates were coated with 10 8 of OMVs secreted by YeS‐c bacteria grown at 4°C, 22°C and 37°C and with OMVs of YeRa‐c, YeRd1‐c and YeRe‐c variants propagated at 37°C. After incubation with/without EDTA, EGTA or EGTA/Mg 2+ (EGTA supplemented with Mg 2+ ions), products of C3 activation were detected with specific antibodies. Data from one of two experiments with similar results are presented. (C) Comparison of complement activation and MBL binding by Yersinia enterocolitica O:3 bacterial cells, LPS and OMVs. ELISA plates were coated with 50 ng/well of bacteria, LPS or OMVs. The deposition of C3 (a, possible AP, CP and LP involvement), C4 (b, possible CP and LP involvement) or C4 LP‐dependent (d) activation products, TCC formation (c, possible AP, CP and LP involvement) and MBL‐binding (e) was analyzed after preincubation with normal human serum (filled columns) or with EDTA‐treated NHS (stripped columns) or without serum (open columns, negative control). Data from one of two experiments with similar results are presented. Dots represent individual OD values for each well. (D) Recognition of Y. enterocolitica O:3 OMVs by human mannose‐binding lectin. YeS‐c_37°C bacteria (1), OMVs (2) and LPS (3) were separated in SDS‐PAGE. After transfer to nitrocellulose and incubation with NHS, the bound MBL was detected with specific mAb (a). The experiment was performed at least 5 times. To control the loading of bacteria, LPS or OMVs the presence of OPS in separated samples was confirmed with anti‐6‐deoxy‐L‐altropyranose mAbs (b).

    Journal: Journal of Extracellular Vesicles

    Article Title: Yersinia enterocolitica O:3 Outer Membrane Vesicles as a Platform for Complement Activation

    doi: 10.1002/jev2.70270

    Figure Lengend Snippet: (A) The impact of OMVs on germicidal activity of serum against YeO3‐c bacteria. The influence of OMVs‐associated with: LPS polysaccharide chain length (a) and pYV‐coded factors (b). Data from one of at least two experiments with the use of separately prepared culture supernatants with similar results are presented. 1 sterile cell culture supernatants (secreted by bacteria grown to OD 600 = 0.6) were used as a source of OMVs; 2 expression at 37°C only; 3 NHS inactivated 30 min at 56°C. (B) Y. enterocolitica O:3 OMV‐induced complement activation in the presence of calcium and magnesium chelators. ELISA plates were coated with 10 8 of OMVs secreted by YeS‐c bacteria grown at 4°C, 22°C and 37°C and with OMVs of YeRa‐c, YeRd1‐c and YeRe‐c variants propagated at 37°C. After incubation with/without EDTA, EGTA or EGTA/Mg 2+ (EGTA supplemented with Mg 2+ ions), products of C3 activation were detected with specific antibodies. Data from one of two experiments with similar results are presented. (C) Comparison of complement activation and MBL binding by Yersinia enterocolitica O:3 bacterial cells, LPS and OMVs. ELISA plates were coated with 50 ng/well of bacteria, LPS or OMVs. The deposition of C3 (a, possible AP, CP and LP involvement), C4 (b, possible CP and LP involvement) or C4 LP‐dependent (d) activation products, TCC formation (c, possible AP, CP and LP involvement) and MBL‐binding (e) was analyzed after preincubation with normal human serum (filled columns) or with EDTA‐treated NHS (stripped columns) or without serum (open columns, negative control). Data from one of two experiments with similar results are presented. Dots represent individual OD values for each well. (D) Recognition of Y. enterocolitica O:3 OMVs by human mannose‐binding lectin. YeS‐c_37°C bacteria (1), OMVs (2) and LPS (3) were separated in SDS‐PAGE. After transfer to nitrocellulose and incubation with NHS, the bound MBL was detected with specific mAb (a). The experiment was performed at least 5 times. To control the loading of bacteria, LPS or OMVs the presence of OPS in separated samples was confirmed with anti‐6‐deoxy‐L‐altropyranose mAbs (b).

    Article Snippet: Depletion of functional C3 from serum was verified in Western blot [acc. to Younger et al. ( )], using goat antibodies against mouse C3 (MP Biomedicals, USA), HRP‐conjugated anti‐goat Ig (Dako) for detection of intact C3 α‐chain and ECL detection system.

    Techniques: Activity Assay, Bacteria, Sterility, Cell Culture, Expressing, Activation Assay, Enzyme-linked Immunosorbent Assay, Incubation, Comparison, Binding Assay, Negative Control, SDS Page, Control

    The requirement of the complement system for Ficolin-A-based immunity. A. The contribution of C3 to hepatic clearance of Spn-19F . Bacteria in the blood (left) and liver/spleen (right) of C3 -/- mice were quantified post i.v. infection with 10 6 (left) or 10 7 CFU (right). n = 3. B. The role of C3 receptors to hepatic clearance of Spn-19F . CRIg -/- , CR3 -/- and CRIg / CR3 -/- mice were infected with 10 6 (left) or 10 7 CFU (right) to quantify bacteria as in (A). n = 3. C. The role of the lectin pathway in hepatic clearance of Spn-19F . Masp1 -/- and Masp2 -/- mice were infected with 10 6 (left) or 10 7 CFU (right) to quantify bacteria as in (A). n = 3. D. Visualization of bacterial capture by KCs of complement-deficient mice. The liver sinusoids of C3 -/- , CRIg / CR3 -/- and Masp2 -/- mice were imaged by intravital microscopy as in 2D. n = 2. E. Complement-dependent bacterial capture by KCs in vitro . Primary mouse KCs were incubated with Spn- 19F in the presence of 10% serum for 30 min. Spn- 14 was used as a negative control. KC-bound bacteria are presented as the percentage of total bacteria. MOI = 1; n = 3-6. F. The importance of the complement system in the protection against Spn- 19F. Various complement-deficient mice were i.v. infected with 10 6 CFU of Spn- 19F and the survival is presented. n = 5. G. The model for the FCN-A-triggered complement-dependent and -independent pathways for bacterial capture by liver macrophages. FCN-A activates C3 on bacterial surface upon binding to the capsule through the lectin pathway. The representative data are presented as mean ± SD, and the statistical differences were determined by Two-way ANOVA with Tukey’s multiple comparisons test (A-C), multiple t tests (D and E) and log-rank test (F). **, P < 0.01; ****, P < 0.0001; ns, no significant difference.

    Journal: bioRxiv

    Article Title: Plasma Ficolins Enable Liver Macrophages to Capture Blood-Borne Bacteria by Recognizing Capsular Polysaccharides

    doi: 10.64898/2025.12.22.696098

    Figure Lengend Snippet: The requirement of the complement system for Ficolin-A-based immunity. A. The contribution of C3 to hepatic clearance of Spn-19F . Bacteria in the blood (left) and liver/spleen (right) of C3 -/- mice were quantified post i.v. infection with 10 6 (left) or 10 7 CFU (right). n = 3. B. The role of C3 receptors to hepatic clearance of Spn-19F . CRIg -/- , CR3 -/- and CRIg / CR3 -/- mice were infected with 10 6 (left) or 10 7 CFU (right) to quantify bacteria as in (A). n = 3. C. The role of the lectin pathway in hepatic clearance of Spn-19F . Masp1 -/- and Masp2 -/- mice were infected with 10 6 (left) or 10 7 CFU (right) to quantify bacteria as in (A). n = 3. D. Visualization of bacterial capture by KCs of complement-deficient mice. The liver sinusoids of C3 -/- , CRIg / CR3 -/- and Masp2 -/- mice were imaged by intravital microscopy as in 2D. n = 2. E. Complement-dependent bacterial capture by KCs in vitro . Primary mouse KCs were incubated with Spn- 19F in the presence of 10% serum for 30 min. Spn- 14 was used as a negative control. KC-bound bacteria are presented as the percentage of total bacteria. MOI = 1; n = 3-6. F. The importance of the complement system in the protection against Spn- 19F. Various complement-deficient mice were i.v. infected with 10 6 CFU of Spn- 19F and the survival is presented. n = 5. G. The model for the FCN-A-triggered complement-dependent and -independent pathways for bacterial capture by liver macrophages. FCN-A activates C3 on bacterial surface upon binding to the capsule through the lectin pathway. The representative data are presented as mean ± SD, and the statistical differences were determined by Two-way ANOVA with Tukey’s multiple comparisons test (A-C), multiple t tests (D and E) and log-rank test (F). **, P < 0.01; ****, P < 0.0001; ns, no significant difference.

    Article Snippet: The C3 deposition on CPSs was detected using a 1:2000 dilution of HRP-conjugated goat IgG antibody against mouse complement C3 (MP Biomedicals) after incubation at 37°C for various durations.

    Techniques: Bacteria, Infection, Intravital Microscopy, In Vitro, Incubation, Negative Control, Binding Assay