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M Ardizzoni

Publications and source records attributed to M Ardizzoni.

2 recordsLinked to original sources

Glycoprotein patterns in Borrelia spp.

The presence of glycoproteins in several Borrelia species was investigated by the digoxigenin labelling technique. The outer surface proteins A and B of seven isolates of the Lyme disease spirochete B. burgdorferi showed to be major glycosylated proteins. Few minor polypeptides with variable molecular masses were also present, at variance, in B. burgdorferi strains. Minor glycosylated proteins with varying molecular masses have been detected in the relapsing fever borreliae B. hermsii, B. turicatae and B. parkeri. B. turicatae showed also a major glycosylated protein with a molecular mass of approximately 40 kDa. Animal pathogenic borreliae B. anserina and B. coriaceae presented only minor glycosylated proteins with variable molecular masses.

Antigens, Bacterial↗

Adherence of Borrelia burgdorferi and Borrelia hermsii to mammalian cells in vitro.

This study investigated the ability of Borrelia burgdorferi and Borrelia hermsii to attach the surface of several types of in vitro-cultured mammalian cells. Borreliae showed different adhesion efficiencies depending on cell type and temperature. Temperatures both lower and higher than 33 degrees and 37 degrees C respectively, decreased the adhesion of borreliae which preferentially adhere to human fibroblast-like cells. The adhesion process, mediated by structures exposed onto the surface of the microorganisms, also proved to be sensitive to the treatment of mammalian cells with hyaluronidase and sialidase, confirming that carbohydrate receptors are involved in the adhesion of borreliae to eukaryotic cells.

Animals↗