Oligosaccharide-receptor interaction of the Galα1-4Gal binding adhesin of Streptococcus suis : Combining site architecture and characterization of two variant adhesin specificities
(1994) In Journal of Biological Chemistry 269(44). p.27466-27472- Abstract
The sugar binding specificities of two groups of Streptococcus suis, a pig pathogen that causes meningitis also in man, were determined. Both the group represented by a recently characterized strain inhibitable by galactose and N-acetylgalactosamine (type PN) and the group inhibitable by galactose (type PO) were found by hemagglutination and solid-phase binding inhibition experiments to recognize the disaccharide Galα1-4Gal of the P1 and Pk blood group antigens. Both types preferred the disaccharide in terminal position. PN showed some, whereas PO showed almost no, binding to the globoside oligosaccharide containing an additional GalNAcβ1-3 residue. The complete... (More)
The sugar binding specificities of two groups of Streptococcus suis, a pig pathogen that causes meningitis also in man, were determined. Both the group represented by a recently characterized strain inhibitable by galactose and N-acetylgalactosamine (type PN) and the group inhibitable by galactose (type PO) were found by hemagglutination and solid-phase binding inhibition experiments to recognize the disaccharide Galα1-4Gal of the P1 and Pk blood group antigens. Both types preferred the disaccharide in terminal position. PN showed some, whereas PO showed almost no, binding to the globoside oligosaccharide containing an additional GalNAcβ1-3 residue. The complete hydrogen bonding patterns were determined by using deoxy and other synthetic derivatives of the receptor disaccharide, and the constructed models of the interactions were compared with that of Escherichia coli PapG396 adhesin. The essential hydroxyls for binding were the HO-4', HO- 6', HO-2, and HO-3 hydroxyls on the β'α-side of the Galα1-4Gal molecule. Type PO adhesin also formed weak interactions with the hydroxyls HO-6 and HO-3'. The mechanism differed from that of E. coli, which binds to a cluster of five hydroxyls (HO-6, HO-2', HO-3', HO-4', and HO-6') and thus to a different part of the receptor disaccharide. These results represent the first example of the comparison of the saccharide receptor hydrogen bonding patterns of two bacterial organisms of different origin and show that the same saccharide may be recognized by two different binding mechanisms.
(Less)
- author
- Haataja, Sauli ; Tikkanen, Kaarina ; Nilsson, Ulf LU ; Magnusson, Göran LU ; Karlsson, Karl-Anders and Finne, Jukka
- organization
- publishing date
- 1994
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 269
- issue
- 44
- pages
- 7 pages
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:7961660
- scopus:0028172418
- ISSN
- 0021-9258
- DOI
- 10.1016/S0021-9258(18)47008-1
- language
- English
- LU publication?
- yes
- id
- 6c2422b5-2879-4dbd-a43b-364f8fa2b482
- date added to LUP
- 2023-02-07 09:54:00
- date last changed
- 2024-04-04 14:47:21
@article{6c2422b5-2879-4dbd-a43b-364f8fa2b482, abstract = {{<p>The sugar binding specificities of two groups of <i>Streptococcus suis</i>, a pig pathogen that causes meningitis also in man, were determined. Both the group represented by a recently characterized strain inhibitable by galactose and N-acetylgalactosamine (type P<sub>N</sub>) and the group inhibitable by galactose (type P<sub>O</sub>) were found by hemagglutination and solid-phase binding inhibition experiments to recognize the disaccharide Galα1-4Gal of the P<sub>1</sub> and P<sup>k</sup> blood group antigens. Both types preferred the disaccharide in terminal position. P<sub>N</sub> showed some, whereas P<sub>O</sub> showed almost no, binding to the globoside oligosaccharide containing an additional GalNAcβ1-3 residue. The complete hydrogen bonding patterns were determined by using deoxy and other synthetic derivatives of the receptor disaccharide, and the constructed models of the interactions were compared with that of <i>Escherichia coli</i> PapG<sub>396</sub> adhesin. The essential hydroxyls for binding were the HO-4', HO- 6', HO-2, and HO-3 hydroxyls on the β'α-side of the Galα1-4Gal molecule. Type P<sub>O</sub> adhesin also formed weak interactions with the hydroxyls HO-6 and HO-3'. The mechanism differed from that of <i>E. coli</i>, which binds to a cluster of five hydroxyls (HO-6, HO-2', HO-3', HO-4', and HO-6') and thus to a different part of the receptor disaccharide. These results represent the first example of the comparison of the saccharide receptor hydrogen bonding patterns of two bacterial organisms of different origin and show that the same saccharide may be recognized by two different binding mechanisms.</p>}}, author = {{Haataja, Sauli and Tikkanen, Kaarina and Nilsson, Ulf and Magnusson, Göran and Karlsson, Karl-Anders and Finne, Jukka}}, issn = {{0021-9258}}, language = {{eng}}, number = {{44}}, pages = {{27466--27472}}, publisher = {{American Society for Biochemistry and Molecular Biology}}, series = {{Journal of Biological Chemistry}}, title = {{Oligosaccharide-receptor interaction of the Galα1-4Gal binding adhesin of <i>Streptococcus suis</i> : Combining site architecture and characterization of two variant adhesin specificities}}, url = {{http://dx.doi.org/10.1016/S0021-9258(18)47008-1}}, doi = {{10.1016/S0021-9258(18)47008-1}}, volume = {{269}}, year = {{1994}}, }