A SIALOGLYCOPROTEIN COMPLEX LINKED TO THE MICROVILLUS CYTOSKELETON ACTS AS A RECEPTOR FOR PILUS (AF/R1) MEDIATED ADHESION OF ENTEROPATHOGENIC ESCHERICHIA-COLI (RDEC-1) IN RABBIT SMALL-INTESTINE

Escherichia coli strain RDEC-1 is an entero-adherent, 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.