Plant PR-5 proteins as mammalian therapeutic agents
The Proteins of the PR-5 family having a lectin-like β barrel domain control apoptosis in yeast through receptor binding. Receptors that specifically bind to PR-5 proteins having a lectin-like β barrel domain have been found to be homologous to mammalian adiponectin receptors, and such PR-5 proteins can act as functional homologues of adiponectin and control adiponectin response in mammals. PR-5 proteins having a lectin-like β barrel domain, for example osmotin, can be used in the treatment of conditions in mammals which are the result of activation or inhibition of adiponectin receptor-mediated metaboloic pathways. PR-5 proteins having a lectin-like β barrel domain, nucleic acids encoding such proteins, and receptors that specifically bind such proteins, can also be used in screening and rational design of new therapeutic agents for use in mammals.
1. A method for identifying an agent that modifies the binding of a PR-5 protein having a lectin-like β barrel domain to an adiponectin receptor in mammalian cells, said method comprising:
combining the PR-5 protein and an adiponectin receptor in the presence or in the absence of a test agent;
determining whether the binding of the PR-5 protein to the adiponectin receptor in the presence or in the absence of the test agent is modified; and
identifying test agents which modify the binding of the PR-5 protein to the adiponectin receptor.
2. The method of claim 1 , wherein the adiponectin receptor is PHO36.
3. The method of claim 1 , wherein the adiponectin receptor is in isolated form.
4. The method of claim 1 , wherein the-adiponectin receptor is expressed in a cell line or tissue culture.
5. The method of claim 4 , wherein the cell line or tissue culture is overexpressing the adiponectin receptor.
6. The method of claim 4 , wherein the adiponectin receptor is expressed in a yeast cell line.
7. The method of claim 6 , wherein the yeast cell line is overexpressing the adiponectin receptor.
8. A method for identifying an agent that modifies the binding of an osmotin protein and a PHO36 receptor, said method comprising:
combining an osmotin protein and a PHO36 receptor in the presence or in the absence of a test agent;
determining whether the binding of the osmotin protein to the PHO36 receptor in the presence or in the absence of the test agent is modified; and
identifying test agents which modify the binding of the osmotin protein to the PHO36 receptor.
9. The method of claim 8 , wherein the PHO36 receptor is in isolated form.
10. The method of claim 8 , wherein the PHO36 receptor is expressed in a cell line or tissue culture.
11. The method of claim 10 , wherein the cell line or tissue culture is overexpressing the PHO36 receptor.
12. The method of claim 10 , wherein the PHO36 receptor is expressed in a yeast cell line.
13. The method of claim 12 , wherein the yeast cell line is overexpressing the PHO36 receptor.