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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
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
2008-07-23 10:01:22
date last changed
2017-08-27 04:04:05
@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},
  volume       = {12},
  year         = {1994},
}