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Argentinean isolates INTA Mo14-4 and INTA 33-5 of Bacillus thuringiensis were characterized. INTA 33-5 (serovar kenyae) had an amorphous crystal containing proteins of 200 and 130 kDa. INTA Mo14-4 (serovar darmstadiensis) had a bipyramidal crystal and a bar-shaped inclusion, containing proteins of 130, 60 and 40 kDa. Crystals of both strains showed no toxicity to lepidopteran, dipteran and coleopteran targets. Trypsin digestion of solubilized crystal proteins of INTA 33-5 produced four peptides (≈65 kDa). No putative δ-endotoxin was detected in Mo14-4. Both isolates showed unique plasmid patterns. Southern analyses showed no homology to four known cursive genes. These results indicate the uniqueness of two novel strains of B. thuringiensis which, in turn, confirm the great diversity of this species.