Affordable Access

Rheumatoid factor autoantibody-binding site: a molecular analysis using monoclonal antibodies with dual anti-TNP and anti-IgG activities.

Authors
  • Reininger, L
  • Spertini, F
  • Shibata, T
  • Jaton, J C
  • Izui, S
Type
Published Article
Journal
European journal of immunology
Publication Date
Nov 01, 1989
Volume
19
Issue
11
Pages
2123–2130
Identifiers
PMID: 2513210
Source
Medline
License
Unknown

Abstract

Two out of five murine IgG3 anti-trinitrophenyl (TNP) monoclonal antibodies (mAb) obtained either by immunization with TNP-keyhole limpet hemocyanin (KLH) (CB1, CB5, CB6 and 4H10) or with dinitrophenyl-lipopolysaccharide (9A6), exhibited anti-IgG rheumatoid factor (RF) activity (CB6 and 4H10). The anti-IgG activity of these two anti-TNP RF was specifically inhibited by murine IgG as well as by the hapten TNP. In order to identify the structural basis for the anti-IgG activity, the nucleotide sequences encoding the VH and VL regions were determined. By comparing the V regions of the non-RF and RF anti-TNP mAb, it was found that one anti-TNP RF antibody, CB6, shares virtually identical VL and VH regions with two anti-TNP antibodies, CB1 and CB5, but markedly differs from these in the D region. Furthermore, the light chain framework region 2 (FR2) and FR3 of non-RF mAb, CB1, CB5 and 9A6, have amino acid sequences almost identical to those claimed for anti-IgG1 RF activity (Shlomchik et al., J. Exp. Med. 1986. 164: 407). Our findings suggest, at least in the case of CB6 mAb, the involvement of CDR, but not light chain FR residues, in IgG binding.

Report this publication

Statistics

Seen <100 times