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. J Cell Biol 1991 Nov;115(4):1021-9
Date
11/01/1991Pubmed ID
1683351Pubmed Central ID
PMC2289956DOI
10.1083/jcb.115.4.1021Scopus ID
2-s2.0-0026332515 (requires institutional sign-in at Scopus site) 29 CitationsAbstract
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.
Author List
Rafiee P, Leffler H, Byrd JC, Cassels FJ, Boedeker EC, Kim YSMESH terms used to index this publication - Major topics in bold
AnimalsBacterial Adhesion
Carbohydrate Metabolism
Cytoskeleton
Electrophoresis, Polyacrylamide Gel
Escherichia coli
Fimbriae, Bacterial
Intestine, Small
Membrane Glycoproteins
Microvilli
Myosins
Platelet Glycoprotein GPIb-IX Complex
Platelet Membrane Glycoproteins
Rabbits
Receptors, Immunologic
Sialoglycoproteins
Solubility
