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PMID: 10403465 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Growth of Viridans streptococci on human serum alpha1-acid glycoprotein.

Journal of dental research ·Vol. 78 ·No. 7 ·1999-07-00 ·Pages 1370-80

Byers HL, Tarelli E, Homer KA, Hambley H, Beighton D

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.

MeSH Terms
Acetylglucosaminidase/metabolism Anions Chromatography, Ion Exchange Glycoside Hydrolases/metabolism Humans Hydrogen-Ion Concentration Mannosidases/metabolism Mass Spectrometry Monosaccharides/metabolism N-Acetylneuraminic Acid/metabolism Neuraminidase/metabolism Opportunistic Infections Orosomucoid/metabolism Polysaccharides/metabolism Streptococcal Infections Streptococcus/enzymology,growth & development,metabolism Streptococcus oralis/enzymology,growth & development,metabolism alpha-L-Fucosidase/metabolism beta-Galactosidase/metabolism
Chemicals
Anions Monosaccharides Orosomucoid Polysaccharides Glycoside Hydrolases Mannosidases Neuraminidase beta-Galactosidase alpha-L-Fucosidase Acetylglucosaminidase N-Acetylneuraminic Acid
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Byers H L
Joint Microbiology Research Unit, Faculty of Clinical Dentistry, King's College School of Medicine and Dentistry, London, United Kingdom.
Tarelli E
Homer K A
Hambley H
Beighton D
Article Info
Journal
Journal of dental research
Abbr.
J Dent Res
ISSN
0022-0345
Published
1999-07-00
Pages
1370-80
Language
English
Region
United States
NLM ID
0354343
Subset
IM
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