Protein H--a surface protein of Streptococcus pyogenes with separate binding sites for IgG and albumin
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1107923
- author
- 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
- organization
- publishing date
- 1994
- 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}}, }