Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Demonstration of separate receptors for human IgA and IgG in group A streptococci type 4. Separation of the solubilized receptors from group- and type-specific antigens, lipoteichoic acid and peptidoglycan

Schalén, C LU orcid ; Christensen, P ; Grubb, A LU orcid ; Samuelsson, G and Svensson, M L (1980) In Acta Pathologica et Microbiologica Scandinavica. Section C, Immunology 88(2). p.77-82
Abstract

The alkaline extract of group A streptococci type 4 was separated by electrophoresis and diffused against 27 normal human sera. One of the precipitates appeared with 85% of the sear. Addition of purified IgA myeloma protein or sera containing IgA M-components to the extract changed the electrophoretic mobility of the precipitate anodically. Purified IgG Fc-fragments or sera containing IgG M-component did not affect the mobility of the precipitate. It was concluded that this precipitate contained the streptococcal receptor for human IgA. A non-precipitating IgG Fc-receptor, with agglutinating capacity for cells coated with human IgG1 but not IgG3, was localized by preparative electrophoresis to the same electrophoretic region as the IgA... (More)

The alkaline extract of group A streptococci type 4 was separated by electrophoresis and diffused against 27 normal human sera. One of the precipitates appeared with 85% of the sear. Addition of purified IgA myeloma protein or sera containing IgA M-components to the extract changed the electrophoretic mobility of the precipitate anodically. Purified IgG Fc-fragments or sera containing IgG M-component did not affect the mobility of the precipitate. It was concluded that this precipitate contained the streptococcal receptor for human IgA. A non-precipitating IgG Fc-receptor, with agglutinating capacity for cells coated with human IgG1 but not IgG3, was localized by preparative electrophoresis to the same electrophoretic region as the IgA receptor. The mobility of the IgG receptor remained unaltered on addition of IgA myeloma protein permitting a separation of the two receptors by preparative electrophoresis. The receptors were distinct from the group specific carbohydrate, peptidoglycan and lipoteicholic acid. No M antigen or opacity factor were demonstrated in the extract.

(Less)
Please use this url to cite or link to this publication:
author
; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
keywords
Antigens, Viral/analysis, Carbohydrates/analysis, Haptoglobins/metabolism, Humans, Immunoglobulin A/metabolism, Immunoglobulin G/metabolism, Lipopolysaccharides, Peptidoglycan/analysis, Phosphatidic Acids/analysis, Receptors, Fc/analysis, Receptors, Immunologic/analysis, Streptococcus pyogenes/analysis, Teichoic Acids/analysis
in
Acta Pathologica et Microbiologica Scandinavica. Section C, Immunology
volume
88
issue
2
pages
77 - 82
publisher
Wiley-Blackwell
external identifiers
  • scopus:0018864724
  • pmid:6992510
ISSN
0304-1328
DOI
10.1111/j.1699-0463.1980.tb00076.x
language
English
LU publication?
yes
id
83ac6f1e-2582-4c95-843c-3d32120e35ec
date added to LUP
2021-10-21 16:11:29
date last changed
2024-01-12 02:57:15
@article{83ac6f1e-2582-4c95-843c-3d32120e35ec,
  abstract     = {{<p>The alkaline extract of group A streptococci type 4 was separated by electrophoresis and diffused against 27 normal human sera. One of the precipitates appeared with 85% of the sear. Addition of purified IgA myeloma protein or sera containing IgA M-components to the extract changed the electrophoretic mobility of the precipitate anodically. Purified IgG Fc-fragments or sera containing IgG M-component did not affect the mobility of the precipitate. It was concluded that this precipitate contained the streptococcal receptor for human IgA. A non-precipitating IgG Fc-receptor, with agglutinating capacity for cells coated with human IgG1 but not IgG3, was localized by preparative electrophoresis to the same electrophoretic region as the IgA receptor. The mobility of the IgG receptor remained unaltered on addition of IgA myeloma protein permitting a separation of the two receptors by preparative electrophoresis. The receptors were distinct from the group specific carbohydrate, peptidoglycan and lipoteicholic acid. No M antigen or opacity factor were demonstrated in the extract.</p>}},
  author       = {{Schalén, C and Christensen, P and Grubb, A and Samuelsson, G and Svensson, M L}},
  issn         = {{0304-1328}},
  keywords     = {{Antigens, Viral/analysis; Carbohydrates/analysis; Haptoglobins/metabolism; Humans; Immunoglobulin A/metabolism; Immunoglobulin G/metabolism; Lipopolysaccharides; Peptidoglycan/analysis; Phosphatidic Acids/analysis; Receptors, Fc/analysis; Receptors, Immunologic/analysis; Streptococcus pyogenes/analysis; Teichoic Acids/analysis}},
  language     = {{eng}},
  number       = {{2}},
  pages        = {{77--82}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{Acta Pathologica et Microbiologica Scandinavica. Section C, Immunology}},
  title        = {{Demonstration of separate receptors for human IgA and IgG in group A streptococci type 4. Separation of the solubilized receptors from group- and type-specific antigens, lipoteichoic acid and peptidoglycan}},
  url          = {{http://dx.doi.org/10.1111/j.1699-0463.1980.tb00076.x}},
  doi          = {{10.1111/j.1699-0463.1980.tb00076.x}},
  volume       = {{88}},
  year         = {{1980}},
}