Abstract
Aeromonas sobria hemolysin is important in the pathogenesis of diarrhoea caused by this enteropathogenic bacterium. By immunoprecipitation analysis using hemolysin and anti-hemolysin antibody, a 66 kDa protein (p66) was identified as a receptor for A. sobria hemolysin on Intestine 407 cells. Treatment of p66 with N-glycosidase F reduced the apparent sized of p66 to 60 kDa on SDS-polyacrylamide gels. p66, released from Intestine 407 cells following incubation with phosphatidylinositol-specific phospholipase C (PI-PLC) treatment, bound A. sobria hemolysin. Thus treatment of Intestine 407 cells with PI-PLC resulted in the remarkable decrease of the sensitivity to A. sobria hemolysin. These results are consistent with the hypothesis that p66, the binding protein for A. sobria hemolysin, is a glycosylphosphatidylinositol-anchored glycoprotein expressed on the surface of Intestine 407 cells and probably plays a role as a receptor for A. sobria hemolysin on the intestinal cells.
Original language | English |
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Pages (from-to) | 215-221 |
Number of pages | 7 |
Journal | Microbial Pathogenesis |
Volume | 27 |
Issue number | 4 |
DOIs | |
Publication status | Published - Oct 1999 |
Externally published | Yes |
Keywords
- Aeromonas sobria
- Glycoprotein receptor
- Hemolysin
- Toxin action
- Toxin receptor
ASJC Scopus subject areas
- Microbiology
- Infectious Diseases