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Growth of Viridans streptococci on human serum alpha1-acid glycoprotein
H L Byers1, E Tarelli, K A Homer
1Joint Microbiology Research Unit, Faculty of Clinical Dentistry, King's College School of Medicine and Dentistry, London, United Kingdom.
Abstract:
Viridans streptococci have emerged as major opportunistic pathogens. We suggest that for these bacteria to proliferate in vivo and cause disease, they must utilize host tissue components. We have therefore examined the ability of all recognized species of viridans streptococci to liberate and utilize the constituent sugars of the glycans of the extensively sialylated human serum alpha1-acid glycoprotein (AGP) as the sole source of carbohydrate to support in vitro growth. Analysis of residual glycans following bacterial growth was performed by high-pH anion exchange chromatography with pulsed amperometric detection and matrix-assisted laser desorption ionization time-of-flight mass spectrometry. Only those species which produced sialidase-namely, Streptococcus oralis, S. intermedius, and S. defectivus--grew on AGP. The extent of degradation of glycans was dependent on the particular glycosidases produced by the bacteria. S. defectivus produced only a sialidase which released the terminal N-acetylneuraminic acid residues of the glycans, and the liberated sugar was utilized. S. intermedius also produced beta-galactosidase and beta-N-acetylglucosaminidase, which removed galactose and N-acetylglucosamine from desialylated glycans, all of which again were utilized by the organism. S. oralis produced beta-galactosidase, beta-N-acetylglucosaminidase, and alpha-fucosidase and novel alpha- and beta-mannosidases which were apparent only from the analysis of the residual sugars of AGP. S. oralis cleaved all the sugars from AGP except for 22% of the N-acetylglucosamine. The residual N-acetylglucosamine residues remaining were those linked to the asparagine of the peptide backbone. All the monosaccharides released by S. oralis from AGP, with the exception of fucose, were utilized. Sialidase production may be a key factor for growth of these species of viridans streptococci on glycoproteins in vivo, since they are commonly associated with extra-oral diseases, with S. oralis emerging as an important pathogen.
Insights
Viridans streptococci use host glycoproteins for growth. Sialidase production is key for opportunistic pathogens like Streptococcus oralis to utilize sugars from human alpha1-acid glycoprotein.
Area of Science:
- Microbiology
- Glycobiology
- Pathogenesis
Background:
- Viridans streptococci are opportunistic pathogens.
- Bacterial proliferation in vivo requires utilization of host components.
- Human serum alpha1-acid glycoprotein (AGP) is a heavily sialylated host glycoprotein.
Purpose of the Study:
- To investigate the ability of viridans streptococci species to utilize AGP glycans.
- To determine the role of glycosidases in nutrient acquisition from AGP.
Main Methods:
- In vitro growth experiments using AGP as the sole carbohydrate source.
- Analysis of residual glycans by high-pH anion exchange chromatography and mass spectrometry.
Main Results:
- Only sialidase-producing species (Streptococcus oralis, S. intermedius, S. defectivus) grew on AGP.
- Degradation extent varied based on glycosidase production.
- S. oralis demonstrated extensive glycan degradation, utilizing most released monosaccharides.
Conclusions:
- Sialidase production is crucial for viridans streptococci to grow on host glycoproteins.
- S. oralis exhibits broad glycan-degrading capabilities, highlighting its pathogenic potential.
- Understanding these mechanisms is vital for combating infections caused by these emerging pathogens.