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Protein H--a surface protein of Streptococcus pyogenes with separate binding sites for IgG and albumin

Frick, Inga-Maria LU ; Åkesson, Per LU ; Cooney, Jakki ; Sjöbring, Ulf LU ; Schmidt, Karl-Hermann ; Gomi, Hideyuki ; Hattori, Shizuo ; Tagawa, Chiaki ; Kishimoto, Fumitaka and Björck, Lars LU (1994) In Molecular Microbiology 12(1). p.143-151
Abstract
Protein H, a molecule expressed at the surface of some strains of Streptococcus pyogenes, has affinity for the constant (IgGFc) region of immunoglobulin (Ig) G. In absorption experiments with human plasma, protein H-sepharose could absorb not only IgG but also albumin from plasma. The affinity constant for the reaction between albumin and protein H was 7.8 x 10(9) M-1, which is higher than the affinity between IgG and protein H (Ka = 1.6 x 10(9) M-1). Fragments of protein H were generated with deletion plasmids and polymerase chain reaction (PCR) technology. Using these fragments in various protein-protein interaction assays, the binding of albumin was mapped to three repeats (C1-C3) in the C-terminal half of protein H. On the albumin... (More)
Protein H, a molecule expressed at the surface of some strains of Streptococcus pyogenes, has affinity for the constant (IgGFc) region of immunoglobulin (Ig) G. In absorption experiments with human plasma, protein H-sepharose could absorb not only IgG but also albumin from plasma. The affinity constant for the reaction between albumin and protein H was 7.8 x 10(9) M-1, which is higher than the affinity between IgG and protein H (Ka = 1.6 x 10(9) M-1). Fragments of protein H were generated with deletion plasmids and polymerase chain reaction (PCR) technology. Using these fragments in various protein-protein interaction assays, the binding of albumin was mapped to three repeats (C1-C3) in the C-terminal half of protein H. On the albumin molecule, the binding site for protein H was found to overlap the site for protein G, another albumin- and IgGFc-binding bacterial surface protein. Also IgGFc-binding could be mapped with the protein H fragments and the region was found N-terminally of the C repeats. A synthetic peptide (25 amino acid residues long) based on a sequence in this region was shown to inhibit the binding of protein H to immobilized IgG or IgGFc. This sequence was not found in previously described IgGFc-binding proteins. However, two other cell surface proteins of S. pyogenes exhibited highly homologous regions. The results identify IgGFc- and albumin-binding regions of protein H and further define and emphasize the convergent evolution among bacterial surface proteins interacting with human plasma proteins. (Less)
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author
; ; ; ; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Molecular Microbiology
volume
12
issue
1
pages
143 - 151
publisher
Wiley-Blackwell
external identifiers
  • pmid:8057834
  • scopus:0028362183
ISSN
1365-2958
DOI
10.1111/j.1365-2958.1994.tb01003.x
language
English
LU publication?
yes
id
3cc60cb3-c527-4a5e-867f-b74f5539e1da (old id 1107923)
date added to LUP
2016-04-01 12:06:25
date last changed
2021-08-29 03:48:02
@article{3cc60cb3-c527-4a5e-867f-b74f5539e1da,
  abstract     = {{Protein H, a molecule expressed at the surface of some strains of Streptococcus pyogenes, has affinity for the constant (IgGFc) region of immunoglobulin (Ig) G. In absorption experiments with human plasma, protein H-sepharose could absorb not only IgG but also albumin from plasma. The affinity constant for the reaction between albumin and protein H was 7.8 x 10(9) M-1, which is higher than the affinity between IgG and protein H (Ka = 1.6 x 10(9) M-1). Fragments of protein H were generated with deletion plasmids and polymerase chain reaction (PCR) technology. Using these fragments in various protein-protein interaction assays, the binding of albumin was mapped to three repeats (C1-C3) in the C-terminal half of protein H. On the albumin molecule, the binding site for protein H was found to overlap the site for protein G, another albumin- and IgGFc-binding bacterial surface protein. Also IgGFc-binding could be mapped with the protein H fragments and the region was found N-terminally of the C repeats. A synthetic peptide (25 amino acid residues long) based on a sequence in this region was shown to inhibit the binding of protein H to immobilized IgG or IgGFc. This sequence was not found in previously described IgGFc-binding proteins. However, two other cell surface proteins of S. pyogenes exhibited highly homologous regions. The results identify IgGFc- and albumin-binding regions of protein H and further define and emphasize the convergent evolution among bacterial surface proteins interacting with human plasma proteins.}},
  author       = {{Frick, Inga-Maria and Åkesson, Per and Cooney, Jakki and Sjöbring, Ulf and Schmidt, Karl-Hermann and Gomi, Hideyuki and Hattori, Shizuo and Tagawa, Chiaki and Kishimoto, Fumitaka and Björck, Lars}},
  issn         = {{1365-2958}},
  language     = {{eng}},
  number       = {{1}},
  pages        = {{143--151}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{Molecular Microbiology}},
  title        = {{Protein H--a surface protein of Streptococcus pyogenes with separate binding sites for IgG and albumin}},
  url          = {{http://dx.doi.org/10.1111/j.1365-2958.1994.tb01003.x}},
  doi          = {{10.1111/j.1365-2958.1994.tb01003.x}},
  volume       = {{12}},
  year         = {{1994}},
}