Recognition of the epidermal growth factor receptor by reovirus.
The demonstration that alpha-sialic acid is the minimal determinant recognized by human reovirus is compatible with the finding that this virus binds to multiple sialoglycoproteins on the host cell surface. However, the identities of these proteins have remained unknown. By applying detergent-solubilized plasma membranes from the human epidermoid carcinoma A431 cell line to immobilized reovirions, we have identified the 150- to 170-kDa epidermal growth factor (EGF) receptor as one of the cell surface proteins recognized by reovirus. Direct interaction between the N-terminal extracellular domain of the EGF receptor and reovirus was confirmed by the demonstration that of a number of proteins secreted by A431 cells, the 105-kDa N-terminal cell surface domain of the EGF receptor was the major protein recognized by the virus. However, as expected, reovirus and EGF did not compete for the same binding site on the EGF receptor of intact A431 cells.
Tang
D
D
Department of Microbiology & Infectious Diseases, University of Calgary Health Sciences Centre, Alberta, Canada.
Strong
J E
JE
Lee
P W
PW
D001345:Autoradiography; D002294:Carcinoma, Squamous Cell; D002462:Cell Membrane / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004815:Epidermal Growth Factor / Q000378:metabolism*; D066246:ErbB Receptors / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D007457:Iodine Radioisotopes; D007700:Kinetics; D008565:Membrane Proteins / Q000302:isolation & purification / Q000378:metabolism; D008970:Molecular Weight; D011991:Receptors, Virus / Q000302:isolation & purification / Q000378:metabolism*; D012087:Reoviridae / Q000502:physiology*; D013462:Sulfur Radioisotopes; D014407:Tumor Cells, Cultured
D007457:Iodine Radioisotopes; D008565:Membrane Proteins; D011991:Receptors, Virus; D013462:Sulfur Radioisotopes; D004815:Epidermal Growth Factor; D066246:ErbB Receptors