Phagocytosis of Escherichia coli mediated by mannose resistant non-fimbrial haemagglutinin (NFA-1).
We examined the interaction between a urinary isolate of E. coli carrying non-fimbrial MR adhesin (NFA-1) and human polymorphonuclear leukocytes (PMN). We found that the organisms attach to PMN and the attachment was dose dependent and saturable. It was inhibited by isolated NFA-1, but not by mannoside. Recombinant plasmid encoding NFA-1 adhesin conferred binding capacity on a non-adhesive strain. The attachment of the bacteria carrying NFA-1 to PMN was associated with oxidative burst and inhibited by isolated NFA-1. The data taken together suggest that NFA-1 mediates the attachment of the bacteria to PMN. The attachment is followed by ingestion and killing of the organisms, but at a slower rate than with bacteria bound via type 1 fimbriae.
Department of Human Microbiology, Sackler School of Medicine, Tel-Aviv University, Ramat Aviv, Israel.
J
J
Goldhar
M
M
Yavzori
Y
Y
Keisari
I
I
Ofek
D018830:Adhesins, Escherichia coli; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics* / Q000378:metabolism; D001667:Binding, Competitive; D002448:Cell Adhesion / Q000235:genetics*; D004926:Escherichia coli / Q000472:pathogenicity*; D010861:Fimbriae, Bacterial / Q000737:chemistry*; D008358:Mannose / Q000378:metabolism; D009504:Neutrophils / Q000276:immunology; D010587:Phagocytosis / Q000276:immunology*; D011994:Recombinant Proteins; D016897:Respiratory Burst
D018830:Adhesins, Escherichia coli; D001425:Bacterial Outer Membrane Proteins; D011994:Recombinant Proteins; D008358:Mannose