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We propose using synthetic microorganisms to help mankind in the creation of habitable worlds by means of terraforming other planets. We deal with the ethical issues our project raises in a report that review the opinion of several experts about the environmental ethics of such a process (see Ethics of Terraforming: A Review).

The prion that we have used in our project does not raise safety issues. It is extremely unlikely that this prion could be pathogenic in humans and it has never been registered in the scientific literature. In fact, the infection of an organism with prions generated in another species hardly ever results in any disease. This effect received the name of “species barrier” and it has been clearly demonstrated that very little differences in the prion amino acidic sequence prevent the transmission between species (Cobb and Surewicz, 2009)). Particularly, it has been observed the existence of a barrier for the transmission of the prion we used in our project between two closely related species as S. cerevisae and C. albicans, although both contain homologue Sup35 proteins (Chien et al., 2004)). The transmission of that prion arise from the formation of amyloid fibrils of the protein Sup35. The NH2-terminus prion-forming domain (PrD or N domain) of that protein from both species has a high N/Q content, associated with amyloid growth in several fungal prions (çwickner et al., 2008)), but it is extremely difficult for Sup35 amyloid of one species to initiate the conformational change in the other. Therefore we can say that the transmission of the prion from yeast to humans, a considerably much less related species than C. albicans, is absolutely impossible. So the human health is not in danger by our project.

In conclusion, our project does not raise safety issues in terms of researcher, public or earth environmental safety. None of the new BioBrick parts that we have made this year (see Submitted BioBricks) raise any safety issue. The strains we have used are not harmful or somehow dangerous for the public, either. So our project is risk-free and can be reproduced on a regular molecular biology laboratory. Finally, there are no special environmental problems for our planet derived from our project.


  • Chien, P., Weissman, J.S., DePace, A.H. (2004). Emerging principles of conformation-based prion inheritance.

Annual Reviews in Biochemestry. 73:617–656.

  • Cobb, N.J., Surewicz, W. K. (2009). Prion diseases and their biochemical mechanisms. Biochemistry. 48: 2574–2585.
  • Wickner, R.B., Shewmaker, F., Kryndushkin, D., Edskes, H.K. (2008). Protein inheritance (prions) based on parallel in-register β-sheet amyloid structures. BioEssays. 30: 955-964.