Collectively, the pathology seen in EMF has been suspected to be mediated via similar Corynoxeine molecular mimicry mechanisms as is seen in Loffler��s and Chaga��s disease. In light of the recent advances towards understanding the mechanism of molecular mimicry seen in Chaga��s disease resulting from resemblance of the C-terminal peptides of T.cruzi ribosomal P proteins to cardiac tissue, we felt it responsive to investigate the potential resemblance of the above various suspected insults in EMF to the same. Both P0 and P2 are a major component of the GTPase center of the large ribosomal subunit. The GTPase center, which is located at the N-termini, and functions as a landing platform for translation factors is regarded as one of the oldest structures in the ribosome and is, presumably, one universally conserved structure in all domains of life. It has been hypothesized that this structure could indeed be responsible for the major breakthrough on the way to the RNA/protein world, since its appearance would have dramatically increased the rate and accuracy of protein synthesis. Notably, one of the most characteristic ribosomal structures is the stalk: a highly flexible and universal lateral protuberance on the large subunit which is directly involved in the interaction of elongation factors, participating in the translocation mechanism. In eukaryotes the stalk is formed by the pentameric complex P0�C 2 2 that is reminiscent of the bacterial complex L10�C4. In particular, the P0 protein is the eukaryotic L10 equivalent and has a key role in the stalk structure. Interestingly, prior studies have actually pointed to conservation of ribosomal proteins from species within the related life Domain. Functionally, these proteins bind to the highly conserved 26S/28S rRNA GTPase center through the N-terminal domain at sites that are equivalent to those found in bacteria. The P0 C-terminal domain, in particular, is known to interact with the acidic phosphoproteins P1 and P2 through their N-terminal domains, forming the tip of the stalk.Consequently, it has been suggested that proteins be regarded as analogous rather than homologous Tenuifolin systems and probably appeared on the ribosomal particle in two independent events in the course of evolution.