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Intracranial Subarachnoidal Route of Infection for Investigating Roles of Streptococcus suis Biofilms in Meningitis in a Mouse Infection Model
Published on: July 1, 2018
Purification of a galactosyl-alpha 1-4-galactose-binding adhesin from the gram-positive meningitis-associated
K Tikkanen1, S Haataja, C François-Gerard
1Department of Biochemistry and Biotechnology, University of Kuopio, Finland.
Abstract:
Streptococcus suis causes meningitis, sepsis, and other serious infections in newborn and young pigs and in adult humans. The Gal alpha 1-4Gal-binding adhesin of S. suis was purified to homogeneity by ultrasonic treatment, fractional ammonium sulfate precipitation, and preparative polyacrylamide gel electrophoresis. Pigeon ovomucoid, a glycoprotein with Gal alpha 1-4Gal terminals, was used to detect the adhesin by blotting. The purified adhesin appeared as single band of an apparent size of 18 kDa and of a pI of 6.4; no disulfide bridges were present. The amount of adhesin as revealed by pigeon ovomucoid binding correlated with the hemagglutination activity of different S. suis strains. The purified adhesin bound to latex particles induced hemagglutination which was specifically inhibited with the same inhibitors as hemagglutination by the intact bacteria, thus demonstrating that the purified protein was the Gal alpha 1-4Gal-recognizing adhesin of S. suis. Two adhesin variants (PN and PO) with differing Gal alpha 1-4Gal binding specificity had the similar electrophoretic mobilities and the same N-terminal peptide sequences, indicating that they were closely related. This represents the first isolation of an adhesin with well-defined cell surface carbohydrate binding activity from Gram-positive bacteria associated with meningitis.
Insights
Researchers isolated the Gal alpha 1-4Gal-binding adhesin from Streptococcus suis, a key factor in meningitis and sepsis. This purified protein confirms its role in bacterial adhesion and infection, paving the way for new therapeutic strategies.
Area of Science:
- Microbiology
- Bacterial Pathogenesis
- Molecular Biology
Background:
- Streptococcus suis is a significant pathogen causing meningitis and sepsis in pigs and humans.
- Bacterial adhesins play a crucial role in the initial stages of infection by mediating attachment to host cells.
- Understanding the specific adhesins involved in S. suis infections is vital for developing targeted interventions.
Purpose of the Study:
- To purify and characterize the Gal alpha 1-4Gal-binding adhesin of Streptococcus suis.
- To confirm the role of the purified adhesin in bacterial hemagglutination and adhesion.
- To investigate the relationship between different adhesin variants.
Main Methods:
- Purification of the adhesin using ultrasonic treatment, ammonium sulfate precipitation, and polyacrylamide gel electrophoresis.
- Detection and characterization of the adhesin using pigeon ovomucoid blotting, SDS-PAGE, and isoelectric focusing.
- Assay of hemagglutination activity and inhibition studies with purified adhesin and intact bacteria.
Main Results:
- The Gal alpha 1-4Gal-binding adhesin was purified to homogeneity, appearing as an 18 kDa protein with a pI of 6.4.
- The purified adhesin demonstrated specific binding to Gal alpha 1-4Gal terminals and induced hemagglutination, inhibited by specific molecules.
- Two adhesin variants (PN and PO) showed similar electrophoretic properties and N-terminal sequences, suggesting close relation.
Conclusions:
- The study successfully isolated and characterized the Gal alpha 1-4Gal-binding adhesin of Streptococcus suis.
- This adhesin is confirmed as the primary factor responsible for Gal alpha 1-4Gal recognition and mediates hemagglutination.
- This is the first isolation of a Gram-positive bacterial adhesin with defined carbohydrate-binding activity from a meningitis-associated pathogen.
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