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Antibody Actions01:26

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Antibodies, or immunoglobulins, are critical players in the immune system's arsenal against invading pathogens. Produced by B cells and plasma cells, their primary role is to detect and bind to specific antigens, molecules found on the surface of pathogens like bacteria or viruses. Beyond antigen recognition, antibodies perform several vital functions that contribute to immune defense.
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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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Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
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Getting oriented with antibodies.

Erik H Klontz1,2, Eric J Sundberg3,2,4

  • 1Institute of Human Virology, University of Maryland School of Medicine, Baltimore, MD 21201, U.S.A.

The Biochemical Journal
|February 5, 2017
PubMed
Summary
This summary is machine-generated.

Two vaccines targeting Neisseria meningitidis serogroup B use recombinant factor H binding protein (fHbp). Antibodies against fHbp are synergistic, activating complement-mediated bacteriolysis through precise Fc domain orientation for enhanced immunotherapy.

Keywords:
Neisseria meningitidisantibodiescrystallographyeffector functionsfactor H binding proteinvaccine

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Area of Science:

  • Immunology
  • Structural Biology
  • Microbiology

Background:

  • Neisseria meningitidis serogroup B causes invasive disease.
  • Recombinant factor H binding protein (fHbp) is a target in new vaccines.
  • Anti-fHbp monoclonal antibodies (mAbs) show synergistic bactericidal activity.

Purpose of the Study:

  • To define the structural basis of synergistic complement activation by mAbs binding to fHbp.
  • To understand how antibody orientation influences effector functions.

Main Methods:

  • X-ray crystallography of fHbp-Fab complexes.
  • Modeling of full-length antibody binding to fHbp.
  • Analysis of Fc domain orientation and distance.

Main Results:

  • Bound antibodies orient their Fc domains 115-130 Å apart.
  • This distance is compatible with multivalent C1q binding.
  • Precise Fc domain orientation is crucial for synergistic complement activation.

Conclusions:

  • The structural basis for synergistic mAb activity against fHbp involves specific Fc domain positioning.
  • This finding has implications for vaccine design and immunotherapy.
  • Precise antibody orientation is a key factor in activating immune effector functions.