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Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
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Identification and structural analysis of dimeric chicken complement component 3d and its binding with chicken

Huan Jin1, Min Tu1, Zhaoying Meng2

  • 1Institute of Animal Husbandry and Veterinary Medicine, Beijing Academy of Agriculture and Forestry Sciences, Beijing, People's Republic of China.

Developmental and Comparative Immunology
|December 7, 2023
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Summary

Chicken complement component 3d (C3d) forms dimers, enhancing its interaction with chicken CR2 (chCR2). This dimerization is key for the chicken immune system

Keywords:
Chicken complement component 3dChicken complement receptor 2DimerHomologous modelingMolecular dockingSurface plasmon resonance

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Area of Science:

  • Immunology
  • Biochemistry
  • Molecular Biology

Background:

  • Complement component 3d (C3d) links innate and adaptive immunity by interacting with CR2.
  • Dimeric human C3d shows enhanced function compared to its monomeric form.
  • The role of dimerization in chicken C3d (chC3d) and its interaction with chicken CR2 (chCR2) remains unexplored.

Purpose of the Study:

  • To investigate whether chicken C3d (chC3d) exhibits dimerization.
  • To determine if dimeric chC3d binds to chicken CR2 (chCR2).
  • To elucidate the interaction mechanisms between chC3d and chCR2.

Main Methods:

  • Coimmunoprecipitation and confocal microscopy to assess chC3d self-interaction and co-localization.
  • Native polyacrylamide gel electrophoresis and western blotting for dimeric chC3d detection.
  • Surface plasmon resonance to quantify the binding affinity (KD) of dimeric chC3d to chCR2.
  • Molecular docking simulations to identify interaction modes.

Main Results:

  • Chicken C3d (chC3d) was confirmed to dimerize.
  • Dimeric chC3d exhibits binding to chicken CR2 (chCR2) with an equilibrium dissociation constant (KD) of 827 nM.
  • Molecular docking revealed that dimeric chC3d can crosslink with the chCR2 receptor.

Conclusions:

  • Chicken C3d (chC3d) shares functional similarities with human C3d, including dimerization.
  • Dimeric chC3d plays a role in interacting with chCR2, potentially bridging innate and adaptive immunity in chickens.
  • These findings provide a foundation for further research into the chicken complement system.