Demonstration of the non-identity between the Fc receptor for human IgG from group A streptococci type 15 and M protein, peptidoglycan and the group specific carbohydrate
Christensen, P ; Grubb, A LU
; Grubb, R
; Samuelsson, G
; Schalén, C
and Svensson, M L
(1979)
In Acta Pathologica et Microbiologica Scandinavica. Section C, Immunology
87C(3).
p.61-257
- Abstract
After electrophoresis of an alkaline extract of type 15 group A streptococci, three main precipitation lines were obtained in diffusion experiments against commercial human polyclonal IgG (lines 1, 2 and 3). Nineteen of 23 sera (83%) from apparently healthy human individuals gave line 3, while 6 of them (26%) gave line 1. The sera giving line 1 did also give line 3. Line 2 was obtained with 2 sera only, also giving lines 1 and 3. Line 3 was caused by a streptococcal Fc-receptor for human IgG, since the line could be displaced by addition of Fc-fragments, but not Fab-fragments of pooled human IgG. Line 1 was shown to be different from line 3, since (1) line 1 was suppressed in contrast to line 3 on absorption of a human serum or... (More)
After electrophoresis of an alkaline extract of type 15 group A streptococci, three main precipitation lines were obtained in diffusion experiments against commercial human polyclonal IgG (lines 1, 2 and 3). Nineteen of 23 sera (83%) from apparently healthy human individuals gave line 3, while 6 of them (26%) gave line 1. The sera giving line 1 did also give line 3. Line 2 was obtained with 2 sera only, also giving lines 1 and 3. Line 3 was caused by a streptococcal Fc-receptor for human IgG, since the line could be displaced by addition of Fc-fragments, but not Fab-fragments of pooled human IgG. Line 1 was shown to be different from line 3, since (1) line 1 was suppressed in contrast to line 3 on absorption of a human serum or commercial polyclonal human IgG with S. aureus; and (2), line 1 was suppressed by Fab-fragments but not Fc-fragments of polyclonal human IgG. Line 2 could be inhibited by addition of peptidoglycan to commercial polyclonal human IgG or a human serum investigated. Another line, 4, obtained in diffusion experiments involving electrophoretically separated alkaline extract of type 15 group A streptococci was type-specific as shown by rabbit antisera to streptococci type M1, M8, M15, and T44, and disappeared on trypsinization of the extract. The component responsible for line 4 in the streptococcal extract, judged to be type-specific M protein, had a mobility different from the component responsible for line 3 in electrophoresis.
(Less)
- author
- Christensen, P
; Grubb, A
LU
; Grubb, R
; Samuelsson, G
; Schalén, C
and Svensson, M L
- organization
- publishing date
- 1979
- type
- Contribution to journal
- publication status
- published
- keywords
- Bacterial Proteins/immunology, Glycoproteins/immunology, Humans, Immunoglobulin Fc Fragments/isolation & purification, Peptidoglycan/immunology, Streptococcus pyogenes/immunology
- in
- Acta Pathologica et Microbiologica Scandinavica. Section C, Immunology
- volume
- 87C
- issue
- 3
- pages
- 61 - 257
- publisher
- Wiley-Blackwell
- external identifiers
-
- pmid:384746
- scopus:0018750452
- ISSN
- 0304-1328
- language
- English
- LU publication?
- yes
- id
- 3761685f-182b-4d77-b401-9a3649b90ea1
- date added to LUP
- 2021-10-16 19:38:50
- date last changed
- 2024-01-12 02:56:36
@article{3761685f-182b-4d77-b401-9a3649b90ea1,
abstract = {{<p>After electrophoresis of an alkaline extract of type 15 group A streptococci, three main precipitation lines were obtained in diffusion experiments against commercial human polyclonal IgG (lines 1, 2 and 3). Nineteen of 23 sera (83%) from apparently healthy human individuals gave line 3, while 6 of them (26%) gave line 1. The sera giving line 1 did also give line 3. Line 2 was obtained with 2 sera only, also giving lines 1 and 3. Line 3 was caused by a streptococcal Fc-receptor for human IgG, since the line could be displaced by addition of Fc-fragments, but not Fab-fragments of pooled human IgG. Line 1 was shown to be different from line 3, since (1) line 1 was suppressed in contrast to line 3 on absorption of a human serum or commercial polyclonal human IgG with S. aureus; and (2), line 1 was suppressed by Fab-fragments but not Fc-fragments of polyclonal human IgG. Line 2 could be inhibited by addition of peptidoglycan to commercial polyclonal human IgG or a human serum investigated. Another line, 4, obtained in diffusion experiments involving electrophoretically separated alkaline extract of type 15 group A streptococci was type-specific as shown by rabbit antisera to streptococci type M1, M8, M15, and T44, and disappeared on trypsinization of the extract. The component responsible for line 4 in the streptococcal extract, judged to be type-specific M protein, had a mobility different from the component responsible for line 3 in electrophoresis.</p>}},
author = {{Christensen, P and Grubb, A and Grubb, R and Samuelsson, G and Schalén, C and Svensson, M L}},
issn = {{0304-1328}},
keywords = {{Bacterial Proteins/immunology; Glycoproteins/immunology; Humans; Immunoglobulin Fc Fragments/isolation & purification; Peptidoglycan/immunology; Streptococcus pyogenes/immunology}},
language = {{eng}},
number = {{3}},
pages = {{61--257}},
publisher = {{Wiley-Blackwell}},
series = {{Acta Pathologica et Microbiologica Scandinavica. Section C, Immunology}},
title = {{Demonstration of the non-identity between the Fc receptor for human IgG from group A streptococci type 15 and M protein, peptidoglycan and the group specific carbohydrate}},
volume = {{87C}},
year = {{1979}},
}