Thin, aggregative fimbriae mediate binding of Salmonella enteritidis to fibronectin.
The binding of human fibronectin and Congo red by an autoaggregative Salmonella enteritidis strain was found to be dependent on its ability to produce thin, aggregative fimbriae, named SEF 17 (for Salmonella enteritidis fimbriae with an apparent fimbrin molecular mass of 17 kDa). Two other fimbrial types produced by S. enteritidis, SEF 14 and SEF 21, were not responsible for the aggregative phenotype or for fibronectin binding. SEF 17-negative TnphoA mutants which retained the ability to produce SEF 14 and SEF 21 were unable to bind human fibronectin or Congo red and lost the ability to autoaggregate. Only purified SEF 17 but not purified SEF 14 or SEF 21 bound fibronectin in a solid-phase binding assay. Furthermore, only SEF 17 was able to inhibit fibronectin binding to S. enteritidis whole cells in a direct competition enzyme-linked immunosorbent assay. These results indicate that SEF 17 are the fimbriae responsible for binding fibronectin by this enteropathogen.
Collinson
S K
SK
Department of Biochemistry and Microbiology, University of Victoria, British Columbia, Canada.
Doig
P C
PC
Doran
J L
JL
Clouthier
S
S
Trust
T J
TJ
Kay
W W
WW
D000469:Alkaline Phosphatase / Q000096:biosynthesis / Q000235:genetics; D001422:Bacterial Adhesion / Q000502:physiology*; D001483:Base Sequence; D016326:Extracellular Matrix Proteins / Q000378:metabolism; D005353:Fibronectins / Q000378:metabolism*; D010861:Fimbriae, Bacterial / Q000378:metabolism*; D008969:Molecular Sequence Data; D016254:Mutagenesis, Insertional; D010641:Phenotype; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis; D012477:Salmonella enteritidis / Q000235:genetics / Q000378:metabolism*
D016326:Extracellular Matrix Proteins; D005353:Fibronectins; D011993:Recombinant Fusion Proteins; D000469:Alkaline Phosphatase