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Complement System

Complement System

The complement system is a group of approximately 20 plasma proteins that strengthen the body's defenses against infections through opsonization, inflammation, and cell lysis. Opsonization involves coating pathogens with complement proteins, making them more recognizable and facilitating phagocyte engulfment. Certain complement proteins induce inflammation that attracts immune cells to the site of infection. Cell lysis involves the destruction of pathogens through the formation of a...

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Related Experiment Video

Updated: Jul 13, 2025

Measuring the 50% Haemolytic Complement CH50 Activity of Serum

Measuring the 50% Haemolytic Complement CH50 Activity of Serum

Published on: March 29, 2010

MAP-2:CD55 chimeric construct effectively modulates complement activation.

Lydia González-Del-Barrio¹, Laura Pérez-Alós¹, Leon Cyranka¹

¹Laboratory of Molecular Medicine, Department of Clinical Immunology, Section 7631, Copenhagen University Hospital, Rigshospitalet, Copenhagen, Denmark.

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology

|October 12, 2023

Summary

This summary is machine-generated.

Engineered fusion proteins, like MAP-2:CD55^1-4, offer potent complement inhibition by targeting multiple pathways. This novel approach shows promise for developing new treatments for complement-driven inflammatory diseases.

Keywords:

CD55 MAP-2 complement inhibition complement regulation lectin pathway

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Published on: July 18, 2017

Area of Science:

Immunology
Protein Engineering

Background:

The complement system is crucial for innate immunity but also implicated in inflammatory diseases.
Current treatments for complement-mediated pathologies are limited.
MAP-2 inhibits the lectin pathway, and CD55 regulates C3/C5 convertase activity.

Purpose of the Study:

To develop a novel chimeric inhibitor, MAP-2:CD55^1-4, targeting multiple complement cascade levels.
To evaluate the in vitro and in vivo efficacy of the chimeric inhibitor compared to its parent molecules.

Main Methods:

Fusion of enzymatically inactive MAP-2 with the N-terminal domains of CD55.
In vitro assessment of complement inhibition across classical, lectin, and alternative pathways.
Hemolytic assays and neutrophil activation studies using Aspergillus fumigatus conidia.

Main Results:

MAP-2:CD55^1-4 demonstrated significantly enhanced inhibition of all three complement pathways compared to MAP-2 or CD55 alone.
The chimeric inhibitor's potency was further increased when complexed with mannose-binding lectin.
MAP-2:CD55^1-4 protected erythrocytes in hemolytic assays and reduced neutrophil activation and phagocytosis.

Conclusions:

Engineered fusion proteins represent a promising strategy for developing potent complement inhibitors.
MAP-2:CD55^1-4 is a highly effective inhibitor with potential therapeutic applications for complement-mediated diseases.