Immunologic Cross-Reactivity of Escherichia Coli B Envelope Glycoproteins with Some Animal and Plant Cell Membrane Proteins

Abstract

Abstract During the past few years a number of laboratories have been investigating the antigenic character of various components of the bacterial envelope. The goals are to develop vaccines against pathogenic organisms (1) and to understand more completely the structural organization of the cell surface (2). We recently reported that rabbit antiserum prepared against isolated envelopes of Escherichia coli B had immunologic reactivity with certain animal cell membrane proteins (3). Specifically, the anti-envelope serum reacted with a “structural protein” preparation from beef heart mitochondria and a phenol soluble protein fraction from the same type of mitochondria. The phenol solubilization technique has been shown to be extremely effective in isolating membrane specific proteins (3), solubilizing membranes such as erythrocyte ghosts which are normally quite resistant to most procedures (4) and preferentially solubilizing glycoproteins (5).