Expression of SEF17 fimbriae by Salmonella enteritidis
- 1 December 1997
- journal article
- Published by Oxford University Press (OUP) in Letters in Applied Microbiology
- Vol. 25 (6) , 447-452
- https://doi.org/10.1111/j.1472-765x.1997.tb00015.x
Abstract
Specific immunological reagents were used to investigate the expression of SEF17 fimbriae by cultured strains of Salmonella enteritidis. Most strains of Salm. enteritidis tested expressed SEF17 when cultured at temperatures of 18-30 degrees C. However, two wild-type strains produced SEF17 when also grown at 37 degrees C and 42 degrees C. Colonization factor antigen agar was the optimum medium for SEF17 expression, whereas Drigalski and Sensitest agars poorly supported SEF17 production. Very fine fimbriae produced by a strain of Salm. typhimurium were specifically and strongly labelled by SEF17 monoclonal and polyclonal antibodies, indicating considerable antigenic conservation between the two. Curli fimbriae from Escherichia coli were similarly labelled. The production of these fimbriae correlated with the binding of fibronectin by the organism. Congo red binding by cultured bacteria was not a reliable criterion for the expression of SEF17 fimbriae.Keywords
This publication has 15 references indexed in Scilit:
- SEF17 fimbriae are essential for the convoluted colonial morphology of Salmonella enteritidisFEMS Microbiology Letters, 1997
- Salmonella enteritidis agfBAC operon encoding thin, aggregative fimbriaeJournal of Bacteriology, 1996
- Characterisation of monoclonal antibodies specific to SEF 21 fimbriae of Salmonella enteritidis and their reactivity with other Salmonellae and EnterobacteriaVeterinary Microbiology, 1996
- Thin, aggregative fimbriae mediate binding of Salmonella enteritidis to fibronectinJournal of Bacteriology, 1993
- Characterisation of monoclonal antibodies against a fimbrial structure of Salmonella enteritidis and certain other serogroup D salmonellae and their application as serotyping reagentsResearch in Veterinary Science, 1992
- The Crl protein activates cryptic genes for curli formation and fibronectin binding in Escherichia coli HB101Molecular Microbiology, 1992
- Thin aggregative fimbriae from diarrheagenic Escherichia coliJournal of Bacteriology, 1992
- Purification and characterization of thin, aggregative fimbriae from Salmonella enteritidisJournal of Bacteriology, 1991
- Expression and Possible Biological Functions of Curli on Infantile Diarrhoea Escherichia coli IsolatesPublished by Springer Nature ,1991
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970