Open AccessCharacterization of fibronectin binding to Salmonella enteritidis strain 27655R
Author(s) -
Baloda Suraj B.
Publication year - 1988
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1988.tb02781.x
Subject(s) - salmonella enteritidis , fimbria , fibronectin , binding site , microbiology and biotechnology , biology , bacterial adhesin , strain (injury) , chemistry , salmonella , biochemistry , cell , escherichia coli , bacteria , gene , genetics , anatomy
The optimal conditions for the binding of fibronectin to Salmonella enteritidis strain 27655R, and the cell‐surface components involved in the binding, were identified. Cultivation on colonisation factor antigen (CFA) agar or in CFA broth at 33°C for 24 h were found to be optimal for the expression of fibronectin binding. Such cultures exhibited 88% and 70% binding of 125 I‐labelled fibronectin and its 29‐kDa N‐terminal domain, respectively. The fibronectin binding was reversed by the addition of unlabelled fibronectin or its 29‐kDa fragment. Scatchard plot analysis of the binding showed that the strain possessed one high‐affinity ( K d = 5.8 × 10 −10 M) and one low‐affinity ( K d = 2 × 10 −8 M) binding site. The fibronectin‐binding could be inhibited by cell surface components of S. enteritidis 27655R released by 30 min treatment at 65°C or 95°C. Inhibition could also be achieved using purified fimbriae. A non‐fimbriated mutant of strain 27655R showed a much reduced binding of fibronectin (15%). Electron microscopic analysis showed association of the gold‐labelled 29‐kDa N‐terminal fragment with S. enteritidis 27655R fimbriae. In conclusion, the findings suggest that S. enteritidis (strain 27655R) possesses fibronectin‐binding fimbriae.