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Related Concept Videos

Complement System01:27

Complement System

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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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Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
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Structure-Guided Engineering of a Complement Component C3-Binding Nanobody Improves Specificity and Adds Cofactor

Henrik Pedersen1, Rasmus Kjeldsen Jensen1, Annette Gudmann Hansen2

  • 1Department of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark.

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Summary

Researchers developed novel nanobodies targeting complement component C3b, a key driver of complement system pathology. The fusion protein EWEnH shows promise for treating complement-driven diseases in vivo.

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Factor Halternative pathwaycomplement systeminhibitorsingle-domain antibody

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Area of Science:

  • Immunology
  • Biochemistry

Background:

  • The complement system is crucial for innate immunity but can cause disease when dysregulated.
  • Complement component C3b is central to complement activation and a therapeutic target.
  • Previous work identified nanobody hC3Nb1 binding to C3 and its products.

Purpose of the Study:

  • To develop novel nanobodies targeting complement C3b for therapeutic applications.
  • To engineer fusion proteins with enhanced specificity and functionality for complement inhibition.

Main Methods:

  • Modification of nanobody hC3Nb1 with a Glu-Trp-Glu motif to create EWE nanobody.
  • Fusion of EWE nanobody with complement Factor H (FH) CCP domains to generate EWEnH and EWEµH.
  • Assays to evaluate binding affinity, Factor I (FI)-mediated cleavage support, and inhibition of complement deposition.

Main Results:

  • EWE nanobody demonstrated specificity for C3 degradation products.
  • EWEnH and EWEµH supported FI-mediated cleavage of human and rat C3b.
  • All tested proteins (EWE, EWEµH, EWEnH) bound C3b and iC3b with high affinity and inhibited alternative pathway complement deposition.
  • EWEnH exhibited excellent solubility and cross-reactivity with human and rat C3b.

Conclusions:

  • Engineered nanobodies, particularly EWEnH, effectively inhibit complement activation.
  • EWEnH demonstrates potential as a therapeutic candidate for in vivo studies in rodent models of complement-mediated diseases.