Demonstration of calcium-induced conformational change(s) in C-reactive protein by using monoclonal antibodies.

Academic Article

Abstract

  • Three out of four anti-C-reactive protein monoclonal antibodies [HB3-2, (micro, k)], EA4-1 (gamma 2a, k) and FB2-1 (gamma 1, k) bind to C-reactive protein in the presence of 2.5 mM Ca2+ but not in the presence of 1.0 mM EDTA, indicating that the conformation of the antigenic determinant(s) recognized by these three antibodies is dependent upon Ca2+. This Ca2+-dependent binding can be inhibited by 1.0 mM phosphocholine, indicating that this antigenic determinant is at or near the phosphocholine-binding site of C-reactive protein. The binding of the fourth monoclonal antibody [HD2-4 (gamma 2-k)] is independent of the presence of Ca2+ and is not inhibited by phosphocholine. HB3-2 (micro, k) recognizes an antigenic determinant on the structurally related proteins, rabbit CRP and serum amyloid P.
  • Published In

    Keywords

  • Antibodies, Monoclonal, Antibody Specificity, C-Reactive Protein, Calcium, Cross Reactions, Edetic Acid, Epitopes, Immunoglobulin G, Phosphorylcholine, Protein Conformation
  • Author List

  • Kilpatrick JM; Kearney JF; Volanakis JE
  • Start Page

  • 1159
  • End Page

  • 1165
  • Volume

  • 19
  • Issue

  • 9