What are the legal and administrative procedures for the examination and granting of patents concerning inventions in biotechnology? Recently, in Jerusalem during a simulation conference, an imaginary patent, covering biologically-engineered 'Human Pink Spider Toxinase' was presented, examined, granted and reviewed^. As well as being a challenge to the imagination, the simulation illustrated the difficulties involved when patenting intellectual property. 'Technical' background In the imaginary country of Narnia^, pink spiders cause 2-3% of deaths in the North Sea Islands. Death is due to a highly poisonous secreted toxin which causes the rapid hemolysis of red blood cells in about 10% of the individuals stung. It was found that victims of the spider lack the activity of a serum enzyme called Human Pink Spider Toxinase (HPST] which, in resistant individuals, causes rapid proteolysis of the toxin and prevents blood hemolysis and, consequently, death. No antidote to the toxin was known. The clinical problems involved with HPST were: how to cure people who are stung; how to identify the sensitivity of individuals prior to their exposure to the dangers of the North Sea Islands; and how to treat them prophylactically so as to avoid their suffering from acute hemolysis if stung by the spider. In order to solve these problems, the gene coding for HPST was cloned, expressed (Fig. 1) and used for restriction fragment length polymorphism (RFLP) studies which aimed at developing a DNA blot diagnosis for HPST deficiency. Hermona Soreq is at the Department of Biological Chemistry, Institute of Life Sciences, The Hebrew University of Jerusalem, 91904 Jerusalem, Israel. The invention: genetically engineered protein possessing the human pink spider toxinase (HPST) activity Preliminary biochemical studies revealed that HPST is a rapidly acting protease with high specificity towards the Pink Spider peptide toxin. HPST is composed of a single subunit thio-protein of 237 amino acid residues with 16 internal S—S bonds. Because of its low concentration in plasma, it was difficult to determine its primary structure by peptide sequencing. However, affinity chromatography on a resin-bound toxin column enabled its purification, although in very small quantities (Fig. 1). The toxin-binding penta-peptide was identified by covalent binding of radioactively labeled toxin analogs, and its sequence was found by micro-sequencing techniques. Oligodeoxynucleotides synthesized according to this sequence^, were labeled and used to screen a liver cDNA library in >igtll phages. The fusion protein which was produced with p-galactosidase in the bacteria containing HPST cDNA, was exceptionally rich in cysteine residues. This property was exploited to detect such clones, by incubating the filters in coumarin maleimide solution. Exposure to UV irradiation resulted in the formation of fluorescence by the thio-protein produced in such bacteria', and the positive clones, previously enriched by hybridization analysis, could thus be confirmed. The cDNA inserts were subjected to DNA sequencing and the toxin-binding pentapeptide sequence was indeed included in them. It was further found that the HPST produced in these bacteria was cata-lytically active and that individuals suffering from HPST deficiency -Fig. 1