
The hydrothermal annelid Alvinella pompejana is considered as one of the most thermotolerant eukaryotes on earth. To survive, it developed numerous physiological adaptations such as an increase of protein thermal properties. In Alvinella, previous in silico analysis showed a significant enrichment in hydrophobic and charged amino acids in its ribosomal proteins. In order to confirm the “thermostable” status of proteins from hydrothermal species, we propose to compare thermo-stability properties, structural characteristics and function of a targeted set of proteins between two hydrothermal annelids (A. pompejana and P. grasslei) and two molluscs (the hydrothermal mussel B. azoricus and the coastal species C. gigas). A complementary analysis of the relation “phenotype-genotype" on three polymorphic systems showing evidences of differential selection to temperature will be conducted on both A. pompejana and C. gigas in natural populations to better understand the effect of thermal selection that could be at the origin of ecological speciation mechanisms.