Cellular receptor molecule

Classical bacterial exotoxins, such as diphtheria toxin, cholera toxin, clostridial neurotoxins, and the anthrax toxins are enzymes that modify their substrates within the cytosol of mammalian cells. To reach the cytosol, these toxins must first bind to different cell-surface receptors and become subsequently internalized by the cells. To this end, many bacterial exotoxins contain two functionally different domains. The binding (B-) domain binds to a cellular receptor and mediates uptake of the enzymatically active (A-) domain into the cytosol, where the A-domain modifies its specific substrate (see Figure 1). Thus, three important properties characterize the mode of action for any AB-type toxin selectivity, specificity, and potency. Because of their selectivity toward certain cell types and their specificity for cellular substrate molecules, most of the individual exotoxins are associated with a distinct disease. Because of their enzymatic nature, placement of very few A-domain molecules in the cytosol will normally cause a cytopathic effect. Therefore, bacterial AB-type exotoxins which include the potent neurotoxins from Clostridium tetani and C. botulinum are the most toxic substances known today. However, the individual AB-type toxins can greatly vary in terms of subunit composition and enzyme activity (see Table 2). 

The HRVs have been divided into the major and minor receptor groups based on two identified cellular receptors [3]. The major group, which is comprised of approximately 90 serotypes, binds to the intercellular adhesion molecule 1 (ICAM-1) [20]. The minor group, about 10 serotypes, binds to the low density lipoprotein receptor family [21]. 

Matthyssee and Phillips (20) isolated two nuclear proteins, from tobacco cells, that bound specifically to 2,4-D. Receptor proteins for auxins, kinetins, and GA have been found (21). Sub-cellular fractions from bean leaves were recently shown to bind abscisic acid (22). Preliminary experiments (22) indicated that maximum ABA binding activity coincides with the activities of membrane-bound Mg -dependent, K+-stimulated ATPase and glucan synthetase. Table I of Biswas and Roy (21) lists hormone receptor proteins reported in plant tissue. For a protein to qualify as a receptor molecule, it should have a high stereo-specific binding capacity (Kd 10 6 to 10 SM) for its particular hormone. In com coleoptiles, both IAA and NAA are equally effective in inducing cell elongations fractions of plasma membrane and endoplasmic reticular membrane contain receptor proteins with Kd values of 10 M to 10 M for auxins (5, 18). When one considers procedural... 

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