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Streptococcus pyogenes type M12 protein shows selective binding to some human immunoglobulin G3 myeloma proteins

Johansson, P J; Malone, C C; Williams, R C Jr; Retnoningrum, D S and Cleary, P P (1994) In Infection and Immunity 62(8). p.3559-3563
Abstract
Purified, recombinant M12 protein from Streptococcus pyogenes CS24 has recently been demonstrated to bind human immunoglobulin G3 (IgG3). The binding site for IgG has been localized to an internal peptide encoded by a PvuII fragment of the gene emm12. We have investigated the ability of an isolated recombinant M12 protein consisting of the peptide encoded by the PvuII fragment to bind various monoclonal human IgG3 myeloma proteins representing a number of both Caucasian and Oriental IgG3 Gm(allotypic) phenotypes. Of nine Caucasian IgG3 myeloma proteins, only two bound strongly to the recombinant M12 protein in enzyme-linked immunosorbent assays. The allotypic phenotypes of the reactive proteins were IgG3m(b+)(g-) and IgG3m(b-)(g+). No... (More)
Purified, recombinant M12 protein from Streptococcus pyogenes CS24 has recently been demonstrated to bind human immunoglobulin G3 (IgG3). The binding site for IgG has been localized to an internal peptide encoded by a PvuII fragment of the gene emm12. We have investigated the ability of an isolated recombinant M12 protein consisting of the peptide encoded by the PvuII fragment to bind various monoclonal human IgG3 myeloma proteins representing a number of both Caucasian and Oriental IgG3 Gm(allotypic) phenotypes. Of nine Caucasian IgG3 myeloma proteins, only two bound strongly to the recombinant M12 protein in enzyme-linked immunosorbent assays. The allotypic phenotypes of the reactive proteins were IgG3m(b+)(g-) and IgG3m(b-)(g+). No binding was seen for seven IgG3 myeloma proteins of Oriental origin with G3m(st+)(u-)(b+)(g-), G3m(st-)(u+)(b+)(g-), G3m(st-)(u+)(b-)(g+), and G3m(st-)(u-)(b-)(g+) phenotypes. The binding of human IgG3 to M12 protein seems to be related to features other than its Gm allotypic markers. Selective reactivity of IgG3 myeloma proteins with M12 protein may provide another way to subclassify human IgG3 molecules. The biological significance of the selective reactivity is not known. (Less)
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author
publishing date
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Contribution to journal
publication status
published
subject
in
Infection and Immunity
volume
62
issue
8
pages
3559 - 3563
publisher
American Society for Microbiology
external identifiers
  • pmid:8039929
  • scopus:0028015950
ISSN
1098-5522
language
English
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no
id
ecaf438d-8aaf-4b86-947d-fbd6c8c6e1fa (old id 1107915)
alternative location
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=302993
date added to LUP
2008-07-23 09:55:28
date last changed
2017-01-01 04:58:22
@article{ecaf438d-8aaf-4b86-947d-fbd6c8c6e1fa,
  abstract     = {Purified, recombinant M12 protein from Streptococcus pyogenes CS24 has recently been demonstrated to bind human immunoglobulin G3 (IgG3). The binding site for IgG has been localized to an internal peptide encoded by a PvuII fragment of the gene emm12. We have investigated the ability of an isolated recombinant M12 protein consisting of the peptide encoded by the PvuII fragment to bind various monoclonal human IgG3 myeloma proteins representing a number of both Caucasian and Oriental IgG3 Gm(allotypic) phenotypes. Of nine Caucasian IgG3 myeloma proteins, only two bound strongly to the recombinant M12 protein in enzyme-linked immunosorbent assays. The allotypic phenotypes of the reactive proteins were IgG3m(b+)(g-) and IgG3m(b-)(g+). No binding was seen for seven IgG3 myeloma proteins of Oriental origin with G3m(st+)(u-)(b+)(g-), G3m(st-)(u+)(b+)(g-), G3m(st-)(u+)(b-)(g+), and G3m(st-)(u-)(b-)(g+) phenotypes. The binding of human IgG3 to M12 protein seems to be related to features other than its Gm allotypic markers. Selective reactivity of IgG3 myeloma proteins with M12 protein may provide another way to subclassify human IgG3 molecules. The biological significance of the selective reactivity is not known.},
  author       = {Johansson, P J and Malone, C C and Williams, R C Jr and Retnoningrum, D S and Cleary, P P},
  issn         = {1098-5522},
  language     = {eng},
  number       = {8},
  pages        = {3559--3563},
  publisher    = {American Society for Microbiology},
  series       = {Infection and Immunity},
  title        = {Streptococcus pyogenes type M12 protein shows selective binding to some human immunoglobulin G3 myeloma proteins},
  volume       = {62},
  year         = {1994},
}