Use of an anti-idiotypic monoclonal antibody in studying amyloidogenic light chains in cells, urine and fibrils: Pathophysiology and clinical implications

V. Bellotti, M. Stoppini, V. Perfetti, I. Zorzoli, G. Marinone, R. Invernizzi, L. M. Zambelli, E. Arbustini, M. Grasso, G. Ferri, E. Ascari, G. Merlini

Research output: Contribution to journalArticlepeer-review

Abstract

A monoclonal anti-idiotype antibody (IgG1k MoAb 3B11D4) raised against the amyloidogenic DEPλ chain dimer binds a conformational idiotope also present on the monoclonal DEP IgA immunoglobulin. MoAb 3B11D4 does not recognize the reduced and alkylated λ chain monomers, nor the 15-17-kDa fibrillar light chain fragments which have the same N-terminal sequence of the urinary light chains. The lack of about 70 amino acid residues of the C terminal of the protein prevents the formation of the self-limiting dimer and may facilitate the deposition of the fragments into amyloid fibrils. MoAb 3B11D4 recognizes the plasma cell clone in bone marrow and 9% of circulating B lymphocytes. Panning experiments demonstrate that this antibody has the capability to selectively eliminate the idiotype positive cells from peripheral blood. Antibodies with these characteristics could become a useful tool for better understanding the pathogenesis of the disease and for new therapeutic options.

Original languageEnglish
Pages (from-to)607-615
Number of pages9
JournalScandinavian Journal of Immunology
Volume36
Issue number4
DOIs
Publication statusPublished - 1992

ASJC Scopus subject areas

  • Immunology

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