Dr. Frasch received his Ph.D. in structural biology from the Faculty of Dentistry, University of Buenos Aires, where he pursued postdoctoral training in parasite biochemistry for a year. Following that experience, he studied parasite molecular biology at the University of Amsterdam and gene cloning at the University of Oregon. He was then appointed a Career Researcher in molecular biology at the National Research Council, and five years later, he began his professorship in molecular genetics at the University of Buenos Aires and his research at the Campomar Foundation. Dr. Frasch received the Luis F. Leloir Award in 1993, he delivered the Wellcome Trust Lecture in London in 1993, and he was the invited speaker at the Year of Louis Pasteur Symposium in Rio de Janeiro in 1995.
TSs have two domains and are encoded in a large gene family.
Furthermore, it was possible to convert the TS into an efficient sialidase by changing only 18 of the 680 amino acid residues in the catalytic domain. Analysis of repetitive domains from other T. cruzi antigens showed that only those present in molecules that are shed into the medium by the parasite stabilize TS in circulation. These repeats were shown to increase the half-life of proteins other than TS and thus might be used to stabilize molecules in the mammalian bloodstream. Research from 1998 Structural and Functional Studies on trans-sialidase and Mucin Families from Trypanosoma cruzi Trypanosoma cruzi requires sialic acid to invade mammalian host cells. TS and NA gene and protein families were analyzed, and members of each family are being used for chimera construction and structural studies to identify the regions involved in the trans -sialidase activity.