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Carbohydrates act as receptors for the periodontitis-associated bacterium Porphyromonas gingivalis: a study of bacterial binding to glycolipids.

Hellström, Ulrika, 2000 (författare)
Gothenburg University,Göteborgs universitet,Odontologiska institutionen, Avdelningen för oral patologi,Institute of Odontology, Department of Oral Pathology
Hallberg, Eva C., 1966 (författare)
Gothenburg University,Göteborgs universitet,Odontologiska institutionen, Avdelningen för oral patologi,Institutionen för laboratoriemedicin, Avdelningen för klinisk kemi/transfusionsmedicin,Institute of Odontology, Department of Oral Pathology,Institute of Laboratory Medicine, Dept of Clinical Chemistry/Transfusion Medicine
Sandros, Jens, 1958 (författare)
Gothenburg University,Göteborgs universitet,Odontologiska institutionen, Avdelningen för oral patologi,Institute of Odontology, Department of Oral Pathology
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Rydberg, Lennart, 1944 (författare)
Gothenburg University,Göteborgs universitet,Institutionen för laboratoriemedicin, Avdelningen för klinisk kemi/transfusionsmedicin,Institute of Laboratory Medicine, Dept of Clinical Chemistry/Transfusion Medicine
Bäcker, Annika E., 1965 (författare)
Gothenburg University,Göteborgs universitet,Odontologiska institutionen, Avdelningen för endodonti med oral diagnostik,Institute of Odontology, Department of Endodontology/Oral Diagnosis
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 (creator_code:org_t)
2004-01-22
2004
Engelska.
Ingår i: Glycobiology. - : Oxford University Press (OUP). - 0959-6658 .- 1460-2423. ; 14:6, s. 511-9
  • Tidskriftsartikel (refereegranskat)
Abstract Ämnesord
Stäng  
  • In this study we show for the first time the use of carbohydrate chains on glycolipids as receptors for the periodontitis-associated bacterium Porphyromonas gingivalis. Previous studies have shown that this bacterium has the ability to adhere to and invade the epithelial lining of the dental pocket. Which receptor(s) the adhesin of P. gingivalis exploit in the adhesion to epithelial cells has not been shown. Therefore, the binding preferences of this specific bacterium to structures of carbohydrate origin from more than 120 different acid and nonacid glycolipid fractions were studied. The bacteria were labeled externally with (35)S and used in a chromatogram binding assay. To enable detection of carbohydrate receptor structures for P. gingivalis, the bacterium was exposed to a large number of purified total glycolipid fractions from a variety of organs from different species and different histo-blood groups. P. gingivalis showed a preference for fractions of human and pig origin for adhesion. Both nonacid and acid glycolipids were used by the bacterium, and a preference for shorter sugar chains was noticed. Bacterial binding to human acid glycolipid fractions was mainly obtained in the region of the chromatograms where sulfated carbohydrate chains usually are found. However, the binding pattern to nonacid glycolipid fractions suggests a core chain of lactose bound to the ceramide part as a tentative receptor structure. The carbohydrate binding of the bacterium might act as a first step in the bacterial invasion process of the dental pocket epithelium, subsequently leading to damage to periodontal tissue and tooth loss.

Ämnesord

MEDICIN OCH HÄLSOVETENSKAP  -- Klinisk medicin -- Odontologi (hsv//swe)
MEDICAL AND HEALTH SCIENCES  -- Clinical Medicine -- Dentistry (hsv//eng)

Nyckelord

Carbohydrate Metabolism
Chromatography
Thin Layer
Periodontitis
microbiology
Porphyromonas gingivalis
growth & development
metabolism
Receptors
Cell Surface
metabolism

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