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Prot Cell    2011, Vol. 2 Issue (4) : 320-332    https://doi.org/10.1007/s13238-011-1029-y      PMID: 21574022
RESEARCH ARTICLE
Interactions of complement proteins C1q and factor H with lipid A and Escherichia coli: further evidence that factor H regulates the classical complement pathway
Lee Aun Tan1,2, Andrew C. Yang3,4, Uday Kishore5,6, Robert B. Sim1,7()
1. Medical Research Council Immunochemistry Unit, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK; 2. Present address: Department of Immunology, Faculty of Medicine, Imperial College London, Hammersmith Hospital, Du Cane Road, London W12 0NN, UK; 3. St Peter’s College, New Inn Hall St., Oxford OX1 2DL, UK; 4. Present address: SUNY Downstate College of Medicine, 450 Clarkson Avenue Brooklyn, NY 11203, USA; 5. Weatherall Institute of Molecular Medicine, John Radcliffe Hospital, University of Oxford, Headington, Oxford OX3 9DS, UK; 6. Present address: Center for Infection, Immunity and Disease Mechanisms, Biosciences, School of Health Sciences and Social Care, Brunel University, Uxbridge UB8 3PH West London, UK; 7. Present address: Department of Pharmacology, University of Oxford, Mansfield Road, Oxford OX1 3QT, UK
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Abstract

Proteins of the complement system are known to interact with many charged substances. We recently characterized binding of C1q and factor H to immobilized and liposomal anionic phospholipids. Factor H inhibited C1q binding to anionic phospholipids, suggesting a role for factor H in regulating activation of the complement classical pathway by anionic phospholipids. To extend this finding, we examined interactions of C1q and factor H with lipid A, a well-characterized activator of the classical pathway. We report that C1q and factor H both bind to immobilized lipid A, lipid A liposomes and intact Escherichia coli TG1. Factor H competes with C1q for binding to these targets. Furthermore, increasing the factor H: C1q molar ratio in serum diminished C4b fixation, indicating that factor H diminishes classical pathway activation. The recombinant forms of the C-terminal, globular heads of C1q A, B and C chains bound to lipid A and E. coli in a manner qualitatively similar to native C1q, confirming that C1q interacts with these targets via its globular head region. These observations reinforce our proposal that factor H has an additional complement regulatory role of down-regulating classical pathway activation in response to certain targets. This is distinct from its role as an alternative pathway downregulator. We suggest that under physiological conditions, factor H may serve as a downregulator of bacterially-driven inflammatory responses, thereby fine-tuning and balancing the inflammatory response in infections with Gram-negative bacteria.
Keywords complement      lipid A      bacteria      factor H      C1q     
Corresponding Author(s): Sim Robert B.,Email:bob.sim@bioch.ox.ac.uk   
Issue Date: 01 April 2011
 Cite this article:   
Lee Aun Tan,Uday Kishore,Robert B. Sim, et al. Interactions of complement proteins C1q and factor H with lipid A and Escherichia coli: further evidence that factor H regulates the classical complement pathway[J]. Prot Cell, 2011, 2(4): 320-332.
 URL:  
https://academic.hep.com.cn/pac/EN/10.1007/s13238-011-1029-y
https://academic.hep.com.cn/pac/EN/Y2011/V2/I4/320
Fig.1  Binding of I-C1q, I-factor H, I-ghA, I-ghB and I-ghC to lipid A, PC and CL-coated wells and liposomes.
(A) Binding of I-C1q, I-factor H, I-ghA, I-ghB and I-ghC to lipid A, PC and CL coated wells. A fixed amount of I-C1q, I-factor H, I-ghA, I-ghB, and I-ghC was incubated with lipid A-coated wells (5 μg lipid A/well) for 1 h at room temperature in VB. The wells were washed, and the amount of bound C1q, factor H, ghA, ghB, and ghC measured. Cardiolipin (CL) served as a positive control while phosphatidylcholine (PC) served as a negative control. Error bars represent standard deviation for five experiments. (B) Binding of I-C1q, I-factor H, I-ghA, I-ghB, and I-ghC to lipid A, PC and CL liposomes. A fixed amount of I-C1q, I-factor H, I-ghA, I-ghB and I-ghC was incubated with lipid A liposomes (10 μg/reaction) for 1 h at room temperature in VB. The liposomes were washed, and the amount of bound C1q, factor H, ghA, ghB and ghC measured. CL served as a positive control while PC served as a negative control. Error bars represent standard deviation for five experiments.
Fig.1  Binding of I-C1q, I-factor H, I-ghA, I-ghB and I-ghC to lipid A, PC and CL-coated wells and liposomes.
(A) Binding of I-C1q, I-factor H, I-ghA, I-ghB and I-ghC to lipid A, PC and CL coated wells. A fixed amount of I-C1q, I-factor H, I-ghA, I-ghB, and I-ghC was incubated with lipid A-coated wells (5 μg lipid A/well) for 1 h at room temperature in VB. The wells were washed, and the amount of bound C1q, factor H, ghA, ghB, and ghC measured. Cardiolipin (CL) served as a positive control while phosphatidylcholine (PC) served as a negative control. Error bars represent standard deviation for five experiments. (B) Binding of I-C1q, I-factor H, I-ghA, I-ghB, and I-ghC to lipid A, PC and CL liposomes. A fixed amount of I-C1q, I-factor H, I-ghA, I-ghB and I-ghC was incubated with lipid A liposomes (10 μg/reaction) for 1 h at room temperature in VB. The liposomes were washed, and the amount of bound C1q, factor H, ghA, ghB and ghC measured. CL served as a positive control while PC served as a negative control. Error bars represent standard deviation for five experiments.
Fig.2  Saturation of I-C1q binding to lipid A-coated wells and lipid A liposomes.
A fixed amount of I-C1q (250 ng per well or per reaction) was mixed with increasing amounts of unlabelled C1q (0-3.75 μg per well or per reaction) in VB and loaded onto lipid A-coated wells or mixed with lipid A liposomes. Saturation of I-C1q binding to lipid A was seen at an input of about 3 μg of C1q. Error bars represent standard deviation for three experiments.
Fig.2  Saturation of I-C1q binding to lipid A-coated wells and lipid A liposomes.
A fixed amount of I-C1q (250 ng per well or per reaction) was mixed with increasing amounts of unlabelled C1q (0-3.75 μg per well or per reaction) in VB and loaded onto lipid A-coated wells or mixed with lipid A liposomes. Saturation of I-C1q binding to lipid A was seen at an input of about 3 μg of C1q. Error bars represent standard deviation for three experiments.
Fig.3  Inhibition of I-C1q binding to lipid A by factor H or by ghA, ghB, and ghC.
A fixed amount of I-C1q in VB (3 μg per well or per reaction) was incubated with various quantities of unlabelled factor H (0-54 μg) either on lipid A-coated wells (A) or with lipid A liposomes (B) at room temperature for 1 h. The wells or liposomes were washed and the amount of bound C1q was determined. Ovalbumin (OVA) was used as a control protein. Error bars represent standard deviation for three experiments (1 μg of factor H is the molar equivalent of 3 μg C1q). Similarly, a fixed amount of I-C1q in VB (3 μg per well or per reaction) was incubated with various quantities of unlabelled ghA, ghB and ghC (0-18 μg) either on lipid A-coated wells (C) or with lipid A liposomes (D) at room temperature for 1 h. The wells or liposomes were washed and the amount of bound C1q was determined as above.
Fig.3  Inhibition of I-C1q binding to lipid A by factor H or by ghA, ghB, and ghC.
A fixed amount of I-C1q in VB (3 μg per well or per reaction) was incubated with various quantities of unlabelled factor H (0-54 μg) either on lipid A-coated wells (A) or with lipid A liposomes (B) at room temperature for 1 h. The wells or liposomes were washed and the amount of bound C1q was determined. Ovalbumin (OVA) was used as a control protein. Error bars represent standard deviation for three experiments (1 μg of factor H is the molar equivalent of 3 μg C1q). Similarly, a fixed amount of I-C1q in VB (3 μg per well or per reaction) was incubated with various quantities of unlabelled ghA, ghB and ghC (0-18 μg) either on lipid A-coated wells (C) or with lipid A liposomes (D) at room temperature for 1 h. The wells or liposomes were washed and the amount of bound C1q was determined as above.
Fig.4  Binding of I-C1q, I-factor H, I-ghA, I-ghB and I-ghC to TG1.
One hundred microliters of VB-0.5 mg/mL ovalbumin containing 125 ng of I-C1q, I-factor H, I-ghA, I-ghB and I-ghC was incubated with 200 μL of (1 × 10 cells/mL in VB-0.5 mg/mL ovalbumin) in 1.7 mL conical ultracentrifuge tubes (blocked overnight with 500 μL of VB-1 mg/mL ovalbumin) and incubated at 37°C for 1 h with mixing every 15 min. Cells were centrifuged and then the radioactivity was counted. Error bars represent standard deviation for five experiments.
Fig.4  Binding of I-C1q, I-factor H, I-ghA, I-ghB and I-ghC to TG1.
One hundred microliters of VB-0.5 mg/mL ovalbumin containing 125 ng of I-C1q, I-factor H, I-ghA, I-ghB and I-ghC was incubated with 200 μL of (1 × 10 cells/mL in VB-0.5 mg/mL ovalbumin) in 1.7 mL conical ultracentrifuge tubes (blocked overnight with 500 μL of VB-1 mg/mL ovalbumin) and incubated at 37°C for 1 h with mixing every 15 min. Cells were centrifuged and then the radioactivity was counted. Error bars represent standard deviation for five experiments.
Fig.5  Saturation and specificity of binding of I-C1q or I-factor H to .
For saturation binding, I-C1q (50 ng/reaction) (A) was mixed with varying quantities of unlabelled C1q in 100 μL of VB-0.5 mg/mL ovalbumin for 1 h on ice. The mixture was then incubated with 200 μL of (1 × 10 cells/mL in VB-0.5 mg/mL ovalbumin) in 1.7 mL conical ultracentrifuge tubes at 37°C for 1 h with mixing every 15 min. Similarly, in (B) I-factor H (50 ng/reaction) was mixed with varying quantities of unlabelled factor H in 100 μL of VB-0.5 mg/mL ovalbumin for 1 h on ice. The reaction mix was then incubated with as above. Cells were centrifuged and then bound radioactivity was counted. Error bars represent standard deviation for three experiments.
Fig.5  Saturation and specificity of binding of I-C1q or I-factor H to .
For saturation binding, I-C1q (50 ng/reaction) (A) was mixed with varying quantities of unlabelled C1q in 100 μL of VB-0.5 mg/mL ovalbumin for 1 h on ice. The mixture was then incubated with 200 μL of (1 × 10 cells/mL in VB-0.5 mg/mL ovalbumin) in 1.7 mL conical ultracentrifuge tubes at 37°C for 1 h with mixing every 15 min. Similarly, in (B) I-factor H (50 ng/reaction) was mixed with varying quantities of unlabelled factor H in 100 μL of VB-0.5 mg/mL ovalbumin for 1 h on ice. The reaction mix was then incubated with as above. Cells were centrifuged and then bound radioactivity was counted. Error bars represent standard deviation for three experiments.
Fig.6  Saturation and specificity of binding of I-ghA, -gh-B, -gh-C to .
I-ghA (A) or I- gh-B (B) or I-gh-C (C) (50 ng/reaction) were mixed with varying quantities of their unlabelled counterparts in 100 μL of VB-0.5 mg/mL ovalbumin for 1 h on ice. The reaction mixtures were then incubated with 200 μL of (1 × 10 cells/mL in VB-0.5 mg/mL ovalbumin) in 1.7 mL conical ultracentrifuge tubes (blocked overnight with 500 μL of VB-1 mg/mL ovalbumin) at 37°C for 1 h with mixing every 15 min. Cells were centrifuged and then the radioactivity was counted. Error bars represent standard deviation for five experiments. To test specificity of binding of I-ghA, I-ghB or I-ghC to (D), I-ghA (1.55 μg), or I-ghB (2.05 μg) or I-ghC (3.05 μg) was incubated with increasing quantities of the corresponding unlabelled ghA, ghB and ghC respectively (or with the negative control, ovalbumin (OVA) in 100 μL of VB-0.5 mg/mL ovalbumin and incubated on ice for 1 h. The mix was added to 200 μL of (1 × 10 cells/mL in VB-0.5 mg/mL ovalbumin) in 1.7 mL eppendorf tubes (blocked overnight with 500 μL of VB - 1 mg/mL ovalbumin) and incubated at 37°C for 1 h with occasional mixing every 15 min. Cells were centrifuged and bound radioactivity was measured. Error bars represent standard deviation for five experiments.
Fig.6  Saturation and specificity of binding of I-ghA, -gh-B, -gh-C to .
I-ghA (A) or I- gh-B (B) or I-gh-C (C) (50 ng/reaction) were mixed with varying quantities of their unlabelled counterparts in 100 μL of VB-0.5 mg/mL ovalbumin for 1 h on ice. The reaction mixtures were then incubated with 200 μL of (1 × 10 cells/mL in VB-0.5 mg/mL ovalbumin) in 1.7 mL conical ultracentrifuge tubes (blocked overnight with 500 μL of VB-1 mg/mL ovalbumin) at 37°C for 1 h with mixing every 15 min. Cells were centrifuged and then the radioactivity was counted. Error bars represent standard deviation for five experiments. To test specificity of binding of I-ghA, I-ghB or I-ghC to (D), I-ghA (1.55 μg), or I-ghB (2.05 μg) or I-ghC (3.05 μg) was incubated with increasing quantities of the corresponding unlabelled ghA, ghB and ghC respectively (or with the negative control, ovalbumin (OVA) in 100 μL of VB-0.5 mg/mL ovalbumin and incubated on ice for 1 h. The mix was added to 200 μL of (1 × 10 cells/mL in VB-0.5 mg/mL ovalbumin) in 1.7 mL eppendorf tubes (blocked overnight with 500 μL of VB - 1 mg/mL ovalbumin) and incubated at 37°C for 1 h with occasional mixing every 15 min. Cells were centrifuged and bound radioactivity was measured. Error bars represent standard deviation for five experiments.
Fig.7  Reciprocal inhibition of I-C1q and factor H binding to .
(A) Inhibition of I-C1q binding to by factor H. A fixed amount of I-C1q in VB (0.55 μg C1q/reaction) was incubated with various quantities of unlabelled purified factor H (0-7.5 μg/reaction) and mixed with (2 × 10 cells/reaction) for 1 h at 37°C. Cells were centrifuged and bound radioactivity was measured (0.185 μg of factor H is the molar equivalent of 0.55 μg of C1q). (B) Inhibition of I-factor H binding to by C1q. Conversely, a fixed amount of I-factor H in VB (0.80 μg factor H/reaction) was incubated with various quantities of unlabelled C1q (0-15 μg/reaction) and mixed with (2 × 10 cells/reaction) for 1 h at 37°C. Cells were centrifuged and bound radioactivity was measured (2.40 μg C1q is the molar equivalent of 0.80 μg factor H). In both experiments, Ovalbumin (OVA) was used as a control protein. Error bars represent standard deviation for three experiments
Fig.7  Reciprocal inhibition of I-C1q and factor H binding to .
(A) Inhibition of I-C1q binding to by factor H. A fixed amount of I-C1q in VB (0.55 μg C1q/reaction) was incubated with various quantities of unlabelled purified factor H (0-7.5 μg/reaction) and mixed with (2 × 10 cells/reaction) for 1 h at 37°C. Cells were centrifuged and bound radioactivity was measured (0.185 μg of factor H is the molar equivalent of 0.55 μg of C1q). (B) Inhibition of I-factor H binding to by C1q. Conversely, a fixed amount of I-factor H in VB (0.80 μg factor H/reaction) was incubated with various quantities of unlabelled C1q (0-15 μg/reaction) and mixed with (2 × 10 cells/reaction) for 1 h at 37°C. Cells were centrifuged and bound radioactivity was measured (2.40 μg C1q is the molar equivalent of 0.80 μg factor H). In both experiments, Ovalbumin (OVA) was used as a control protein. Error bars represent standard deviation for three experiments
Fig.8  Assessment of C4 deposition on lipid A-coated wells.
C1q and factor H-depleted serum, repleted with various molar ratios of C1q and factor H, were incubated in lipid A-coated wells for 1 h at 37°C. The depleted serum is essentially completely C1q-deficient, but only 75% factor H depleted. Repletion was done by adding a fixed quantity of C1q and a variable quantity of factor H to the depleted serum. This was achieved by mixing 13 μL of depleted serum with 87 μL of VB containing 0.9 μg C1q and 0.9-21.6 μg of factor H. The lipid A-coated wells were washed and the relative amount of C4 deposition was determined. Error bars represent standard deviation for five experiments. “Control serum” is the depleted serum with no addition of C1q or factor H.
Fig.8  Assessment of C4 deposition on lipid A-coated wells.
C1q and factor H-depleted serum, repleted with various molar ratios of C1q and factor H, were incubated in lipid A-coated wells for 1 h at 37°C. The depleted serum is essentially completely C1q-deficient, but only 75% factor H depleted. Repletion was done by adding a fixed quantity of C1q and a variable quantity of factor H to the depleted serum. This was achieved by mixing 13 μL of depleted serum with 87 μL of VB containing 0.9 μg C1q and 0.9-21.6 μg of factor H. The lipid A-coated wells were washed and the relative amount of C4 deposition was determined. Error bars represent standard deviation for five experiments. “Control serum” is the depleted serum with no addition of C1q or factor H.
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