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- Title
Two Human IgM Myeloma Proteins with Unusual Specificities for Streptococcal Carbohydrate-Associated Epitopes.
- Authors
Emmrich, F.; Bundle, D.; van der Zee, J.; Out, T.; Zenke, G.; Eichmann, K.
- Abstract
Five hundred and fifty human sera from patients with IgM myeloma or Waldenström's macroglobulinaemia were screened by a solid-phase enzyme-linked immunoassay for binding to the carbohydrate of group A streptococci (A-CHO). Two of them (AC8 and AC179) contained immunoglobulin, which bound specifically to A-CHO even at serum dilutions of 1 : 107. Using synthetic oligosaccharides coupled to protein for inhibition studies, the fine specificities of AC8 and AC179 were determined. AC179 is directed to α-linked rhamnose oligosaccharides. AC8 appears to be specific for N-acetyl-D-glucosamine (GleNAc) side chains β(1→2)-linked to rhamnose, whereas GlcNAc side chains in A-CHO are reported to be β(1→3)-linked to the rhamnose backbone. Naturally occurring anti-A-CHO antibodies consist mainly of low-affinity antibodies to such β (1→3)-linked GlcNAc. In contrast, both myeloma antibodies show more than 10 times higher relative affinities to A-CHO than antibodies prepared from normal human serum (anti-GlcNAc and anti-A-CHO, respectively) by selection for high affinity in the elution procedure. AC179 induced complement activation in the presence of A-CHO.
- Subjects
IMMUNOGLOBULIN M; MYELOMA proteins; TUMOR proteins; CARBOHYDRATES; EPITOPES; HUMAN body
- Publication
Scandinavian Journal of Immunology, 1985, Vol 21, Issue 2, p119
- ISSN
0300-9475
- Publication type
Article
- DOI
10.1111/j.1365-3083.1985.tb01410.x