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Related Experiment Videos

Ig N-glycan orientation can influence interactions with the complement system

K D White1, R D Cummings, F J Waxman

  • 1Department of Microbiology, University of Oklahoma Health Sciences Center, Oklahoma City 73104, USA.

Journal of Immunology (Baltimore, Md. : 1950)
|January 1, 1997
PubMed
Summary
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Antibody N-glycan orientation, not composition, affects lectin binding and complement activation. Accessible N-glycans can inhibit complement C1q binding, influencing immune responses.

Area of Science:

  • Immunology
  • Glycobiology
  • Structural Biology

Background:

  • Monoclonal antibodies (mAbs) of the IgG2a isotype can exhibit distinct lectin-binding properties despite similar monosaccharide content.
  • These differences are often attributed to variations in N-glycan structure, but conformational factors may also play a role.

Purpose of the Study:

  • To investigate whether the conformational accessibility of N-glycans on IgG2a mAbs influences their lectin-binding properties and subsequent complement activation.
  • To determine the impact of N-glycan orientation on the interaction between antibodies and the complement system.

Main Methods:

  • Comparative analysis of lectin binding to two dinitrophenyl-specific murine IgG2a mAbs with similar N-glycan monosaccharide composition.
  • Enzymatic assays using beta-1,4-galactosyltransferase and peptide N-glycosidase F to assess N-glycan accessibility.

Related Experiment Videos

  • Assessment of complement activation (C1q, C4b, C3b deposition) following enzymatic deglycosylation or in factor B-depleted serum.

    • Main Results:

    • Differential lectin binding was observed and lost upon antibody denaturation, indicating conformational dependence.
    • N-glycan accessibility correlated with reactivity to enzymes and lectin binding.
    • Greater N-glycan accessibility was inversely related to the capacity to activate the classical complement pathway.
    • Enzymatic removal of accessible N-glycans enhanced complement deposition, while removal of less accessible N-glycans inhibited it.

    Conclusions:

    • The orientation and conformational accessibility of N-glycans on IgG2a antibodies significantly impact their interaction with lectins and the complement system.
    • N-glycan conformation, rather than just composition, plays a crucial role in modulating antibody effector functions, particularly classical complement pathway activation.