Monoclonal antibody as a probe for structure and function of an Escherichia coli outer membrane protein.
Eight independently derived monoclonal antibodies directed against the LamB protein were produced and characterized. By using these antibodies as probes, we identified four distinct topological and functional regions in the LamB molecule. Four monoclonal antibodies recognize antigenic determinants of the protein exposed on the outer side of the membrane. Two of these have their binding sites located in a region involved in maltose transport. One monoclonal antibody presumably binds to a determinant which is normally hidden in the membrane and three monoclonal antibodies recognize determinants facing the periplasmic space.
D000818:Animals; D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D001425:Bacterial Outer Membrane Proteins; D010582:Bacteriophage lambda / Q000378:metabolism*; D001667:Binding, Competitive; D002462:Cell Membrane / Q000276:immunology; D000939:Epitopes / Q000032:analysis; D004926:Escherichia coli / Q000276:immunology*; D005455:Fluorescent Antibody Technique; D006825:Hybridomas / Q000276:immunology; D007700:Kinetics; D051379:Mice; D008807:Mice, Inbred BALB C; D018272:Porins; D011991:Receptors, Virus / Q000276:immunology* / Q000378:metabolism
D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D001425:Bacterial Outer Membrane Proteins; D000939:Epitopes; D018272:Porins; D011991:Receptors, Virus; C016532:maltoporins