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Oligosaccharide-receptor interaction of the Galα1-4Gal binding adhesin of Streptococcus suis : Combining site architecture and characterization of two variant adhesin specificities

Haataja, Sauli ; Tikkanen, Kaarina ; Nilsson, Ulf LU ; Magnusson, Göran LU ; Karlsson, Karl-Anders and Finne, Jukka (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.

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organization
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Contribution to journal
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published
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in
Journal of Biological Chemistry
volume
269
issue
44
pages
7 pages
publisher
American Society for Biochemistry and Molecular Biology
external identifiers
  • scopus:0028172418
  • pmid:7961660
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}},
}