Modern Complement Analysis

Kirschfink, Michael; Mollnes, Tom Eirik

doi:10.1128/cdli.10.6.982-989.2003

Cited by 69 publications

(49 citation statements)

References 74 publications

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“…Anti-C5 mAb was used in Wang et al's article entitled “anti-C5 monoclonal antibody therapy prevents collagen induced arthritis and ameliorates established disease” and was shown to diminish terminal complement activation. 26-29 C5 mAb binds specifically to the C5 beta chain between residues Tyr334 and Lys41, while C5a mAb binds to a neo-epitope on human C5a/C5a des-Arg. The monoclonal antibody directed against C5b reacts with an epitope present on C5b as well as on C5.…”

Section: Resultsmentioning

confidence: 99%

Inhibitors of C5 complement enhance vaccinia virus oncolysis

et al. 2013

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Genetically engineered tumor-selective vaccinia virus (VV) has been demonstrated to be a highly effective oncolytic agent, but immune clearance may limit its therapeutic potential. As previously demonstrated, immunosuppression can lead to significant enhancement of viral recovery and therapeutic effect, but the magnitude of complement-mediated viral inactivation has not been fully elucidated and warrants further investigation. Using fluorescent microscopy and quantitative plaque assays, we have determined complement's key role in viral clearance and its multi-faceted means to pathogen destruction. Complement can lead to direct viral destruction and inhibition of viral uptake into cells, even in the absence of anti-vaccinia antibodies. Our data demonstrate C5 to be integral to the clearance pathway, and its inhibition by Staphylococcal superantigen-like protein (SSL7) leads to a 90-fold and 150-fold enhancement of VV infectivity in both the presence and absence of anti-VV antibodies, respectively. This study suggests that complement inhibition may reduce vaccinia viral neutralization and may be critical to future in vivo work.

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Section: Resultsmentioning

confidence: 99%

Inhibitors of C5 complement enhance vaccinia virus oncolysis

et al. 2013

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“…Liu and Young described an assay performed in wells of microtiter plates in which the readout is the turbidity in the sample; a low turbidity is correlated with a high degree of lysis of the erythrocytes (27). More recently, alternative assays for evaluation of complement function have been introduced, but they have not yet assumed a full role in the clinic (7,10,20,24,29,46).…”

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confidence: 99%

Use of Serum or Buffer-Changed EDTA-Plasma in a Rapid, Inexpensive, and Easy-To-Perform Hemolytic Complement Assay for Differential Diagnosis of Systemic Lupus Erythematosus and Monitoring of Patients with the Disease

Ekdahl

Norberg

Bengtsson

et al. 2007

Clin Vaccine Immunol

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We previously described a simplified quantitative hemolytic assay for classical pathway (CP) hemolytic function in serum that has been shown to correlate with the 50% hemolytic complement (CH 50 ) assay. In the present study, we used this assay to compare CP functions; plasma levels of C3, C4, and C3dg; and ratios of C3dg to C3 in healthy individuals and patients with systemic lupus erythematosus (SLE) or rheumatoid arthritis (RA) with different degrees of complement activation. A significant depression in CP function and levels of C4 and C3 and increased C3dg levels and C3dg/C3 ratios were observed in the SLE patients. In patients with RA, CP function was normal, whereas C3, C4, and C3dg levels and the C3dg/C3 ratio were elevated. The SLE results are compatible with systemic complement consumption, whereas the RA data suggest an acute-phase reaction with a normal C3 catabolic rate. To facilitate the handling of patient samples, we also developed a method to restore the hemolytic function of EDTA-plasma by transferring it to Veronal-buffered saline containing the thrombin inhibitor lepirudin. This process inhibits coagulation and enables complement activation, allowing a longer time lag between sample harvesting and testing. These results, combined with previous correlation studies, suggest that the CP hemolytic assay can effectively replace the CH 50 assay for routine SLE differential diagnosis and monitoring of disease activity.

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“…However, although this assay is very suitable for functional studies of complement activities in vitro, it only allows for semi-quantitative assessments with respect to the estimation of individual complement factors. 21 Further quantification of C3, C4 and C5 revealed the strongest reduction of C5 in FK778-treated probes without relevant effects on C3 and C4. The involved pathway remains unclear but one possibility might be that inactivation/degradation of C5 by C5-convertase could be triggered.…”

Section: Discussionmentioning

confidence: 98%