Linked Life Data

10403465

Source:http://linkedlifedata.com/resource/pubmed/id/10403465

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1999-7-29
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
D
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0022-0345
pubmed:author
pubmed:issnType
Print
pubmed:volume
78
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1370-80
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:10403465-Acetylglucosaminidase, pubmed-meshheading:10403465-Anions, pubmed-meshheading:10403465-Chromatography, Ion Exchange, pubmed-meshheading:10403465-Glycoside Hydrolases, pubmed-meshheading:10403465-Humans, pubmed-meshheading:10403465-Hydrogen-Ion Concentration, pubmed-meshheading:10403465-Mannosidases, pubmed-meshheading:10403465-Mass Spectrometry, pubmed-meshheading:10403465-Monosaccharides, pubmed-meshheading:10403465-N-Acetylneuraminic Acid, pubmed-meshheading:10403465-Neuraminidase, pubmed-meshheading:10403465-Opportunistic Infections, pubmed-meshheading:10403465-Orosomucoid, pubmed-meshheading:10403465-Polysaccharides, pubmed-meshheading:10403465-Streptococcal Infections, pubmed-meshheading:10403465-Streptococcus, pubmed-meshheading:10403465-Streptococcus oralis, pubmed-meshheading:10403465-alpha-L-Fucosidase, pubmed-meshheading:10403465-beta-Galactosidase
pubmed:year
1999
pubmed:articleTitle
Growth of Viridans streptococci on human serum alpha1-acid glycoprotein.
pubmed:affiliation
Joint Microbiology Research Unit, Faculty of Clinical Dentistry, King's College School of Medicine and Dentistry, London, United Kingdom.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't