Artigo Revisado por pares

A human monoclonal IgMλ specific for an epitope shared by the 200 kDa neurofilament protein, histones and ribosomal proteins

1995; Elsevier BV; Volume: 8; Issue: 6 Linguagem: Inglês

10.1016/s0896-8411(95)80026-3

ISSN

1095-9157

Autores

I. Brindel, J L Preud'homme, Jean‐Jacques Diaz, C. Giraud, Jean-Michel Vallat, Marie‐Odile Jauberteau,

Tópico(s)

Skin and Cellular Biology Research

Resumo

Serum monoclonal IgMλ from a patient with axonal neuropathy reacted with axonal, nuclear, cytoplasmic and cell surface components by immunofluorescence. Experiments performed with Fab fragments of the monoclonal IgM proved that this reactivity was clearly due to actual antibody activity. Further study by Western blotting and ELISA showed that the IgMλ reacted with the 200 kDa neurofilament protein, H1 and H2b histones and L14, L24 and L7 ribosomal proteins. This reactivity was abolished after adsorption either on purified 200 kDa neurofilament protein or on ribosomal proteins, demonstrating that these reactive proteins share a common epitope which possibly reflects sequence similarities. Sequence homology pointed to the involvement of the peptide AKSPEKAK in the epitope, and this was confirmed by dot blot analysis and adsorption experiments with this peptide. In addition, monoclonal IgM showed low level polyreactivity.

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