Showing papers by "Hakon Leffler published in 1991"
TL;DR: The results demonstrate the importance of fitness between host receptors and bacterial adhesins for infection and suggest that minor receptor epitope differences have profound effects on the disease process.
Abstract: Escherichia coli strains which colonize the human urinary tract express lectins specific for different members of the globoseries of glycolipids, e.g., globotetraosylceramide and globo-A. This study investigated the importance of globo-A expression for attachment to human uroepithelial cells, colonization of the urinary tract, and severity of urinary tract infection. The expression of receptor-active glycolipids by erythrocytes and epithelial cells was analyzed by thin-layer chromatography and bacterial overlay as well as by bacterial binding to those cells. The epithelial expression of the globo-A receptor was restricted to individuals of blood group A with a positive secretor state. Consequently, globo-A binding E. coli strains attached only to epithelial cells from these individuals. In contrast, globoside-recognizing strains attached in similar numbers to uroepithelial cells regardless of the ABH blood group and secretor state of the donor. The role of host receptor expression for infection with globo-A-specific E. coli was analyzed in 1,473 children with urinary tract infections. All those infected with strains exclusively expressing globo-A-specific adhesins were found to be of blood group A, compared with 45% in the population at large (P less than 0.006). The inflammatory response (fever, C-reactive protein, erythrocyte sedimentation rate) of individuals infected with these strains was lower than that in individuals with infections caused by globoside binding strains. The results demonstrate the importance of fitness between host receptors and bacterial adhesins for infection and suggest that minor receptor epitope differences have profound effects on the disease process. Images
108 citations
TL;DR: It is shown that deglycosylation of the purified glycoprotein results in loss of receptor activity, suggesting that unsubstituted lactosamine units, including the 6-antenna of the major oligosaccharide, mediate F. nucleatum adherence.
91 citations
TL;DR: The cloning and sequencing of a cDNA encoding the human galactoside-binding lectin from a breast carcinoma is reported, which encodes a protein of 250 amino acids that is over 80% identical to its mouse and rat counterparts.
80 citations
TL;DR: It is demonstrated that RDEC-1 binds, via AF/R1 pili, to a specific rabbit ileal microvillus membrane glycoprotein receptor complex of subunits 130 and 140 kD, which suggests that, in addition to this function in mucosal adherence, the pili may facilitate subsequent (second stage) close effacing attachment of RD EC-1 to the host epithelium by influencing cytoskeletal function.
Abstract: Escherichia coli strain RDEC-1 is an enteroadherent, diarrheagenic pathogen in rabbits that utilizes AF/R1 pili for initial (stage 1) adherence, but the host receptors for this adhesion are unknown. Here we demonstrate that RDEC-1 binds, via AF/R1 pili, to a specific rabbit ileal microvillus membrane glycoprotein receptor complex of subunits 130 and 140 kD. The binding involves sialic acid present on oligosaccharide moieties of the glycoprotein receptor. Furthermore, the microvillus membrane glycoprotein receptor complex appears to be associated with cytoskeletal components via brush border myosin 1. This newly described link between AF/R1 receptor and cytoskeletal components suggests that, in addition to this function in mucosal adherence, the pili may facilitate subsequent (second stage) close effacing attachment of RDEC-1 to the host epithelium by influencing cytoskeletal function.
34 citations