Open AccessBinding of purified Escherichia coli O75X adhesin to frozen sections of human kidney
Author(s) -
Korhonen Timo K.,
Virkola Ritva,
VäisänenRhen Vuokko,
Holthöfer Harry
Publication year - 1986
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.1574-6968.1986.tb01549.x
Subject(s) - bacterial adhesin , glomerulus , nephron , biology , escherichia coli , basement membrane , antibody , antigen , microbiology and biotechnology , kidney , chemistry , biochemistry , immunology , endocrinology , gene
Binding characteristics of the purified Escherichia coli O75X adhesin in frozen sections of human kidney were determined, using antibodies raised against the purified antigen and rhodamine‐conjugated second antibodies. To identify the adhesin‐binding nephron domains, the same tissue sections were double stained with fluorescein isothiocynate‐conjugated nephron site‐specific lectins. The results revealed that, at the tubular pole, the O75X adhesin bound selectively to the basement membrane of proximal and distal tubules and, with a slightly lower efficiency, of collecting ducts. In the glomerulus, the O75X adhesin bound only to the parietal epithelial cells (Bowman's capsule). The purified O75X adhesin bound also to exfoliated epithelial cells in human urine. Our results suggest that the O75X adhesin may contribute to the uropathogenicity of E. coli by binding the bacteria to tissue structures in the human urinary tract.