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Activating B cell signaling with defined multivalent ligands.

Erik B Puffer1, Jason K Pontrello, Jessica J Hollenbeck

  • 1Department of Biochemistry,University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.

ACS Chemical Biology
|April 17, 2007
PubMed
Summary
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High-valency antigens synthesized using ring-opening metathesis polymerization (ROMP) trigger antibody production by activating B cell antigen receptor (BCR) signaling. This indicates antigen valency is critical for initiating immune responses.

Area of Science:

  • Immunology
  • Biochemistry
  • Polymer Chemistry

Background:

  • B lymphocytes mediate immunity and tolerance via B cell antigen receptor (BCR) signaling.
  • Antigen valency is a proposed, yet understudied, factor influencing BCR signaling outcomes.

Purpose of the Study:

  • To investigate the role of antigen valency in B cell activation and signaling.
  • To synthesize and utilize multivalent ligands of defined valencies for B cell studies.

Main Methods:

  • Synthesis of multivalent ligands with controlled valencies using ring-opening metathesis polymerization (ROMP).
  • In vivo administration of ROMP-generated multivalent antigens to mice.
  • Analysis of BCR clustering, membrane microdomain localization, intracellular Ca2+ concentration, and BCR internalization.

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Main Results:

  • High-valency ROMP antigens elicited antibody production in vivo.
  • All tested multivalent antigens activated BCR signaling.
  • BCR clustering, microdomain localization, and Ca2+ flux increased with antigen valency.
  • BCR internalization was independent of antigen valency.
  • Unligated BCRs clustered with ligated BCRs, suggesting signal amplification.

Conclusions:

  • Antigen valency is a key determinant of B cell immune responses, with high valency required for antibody production.
  • The ability to increase intracellular Ca2+ concentration is directly linked to antigenicity.
  • BCR signal amplification occurs through receptor array formation.