Possible role of ?-1-microglobulin in mediating bacterial attachment to model surfaces

✍ Scribed by Wassall, M. A. ;Santin, M. ;Peluso, G. ;Denyer, S. P.

• Publisher: John Wiley and Sons
• Year: 1998
• Tongue: English
• Weight: 290 KB
• Volume: 40
• Category: Article
• ISSN: 0021-9304
• DOI: 10.1002/(sici)1097-4636(19980605)40:3<365::aid-jbm4>3.0.co;2-d

✦ Synopsis

Urine proteins in the molecular weight range of 9-137 kDa deposit to an equal extent from pooled human urine onto glass (12.7 ± 1.9 g/cm) and polystyrene (11.8 ± 1.8 g/cm). Selective desorption of the proteins was achieved by washing with water or water/isopropanol mixtures. Irrespective of the washing process, proteins of molecular weight greater than 90 kDa remained associated with both surfaces while water washings alone removed most low molecular weight material. A 29 kDa protein, ␣-1microglobulin, was removed from glass by water washing but required a 30% (v/v) isopropanol wash to desorb from polystyrene, implying attachment via hydrophobic bonding. The adhesion to polystyrene surfaces of Pseudomonas aeruginosa B4, a clinical isolate from a urinary tract infection (UTI), was strongly associated with the presence of ␣-1microglobulin, which may be acting as a mediator of bacterial adhesion.