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Blood, Vol. 93 No. 6 (March 15), 1999:
pp. 2025-2032
Tandem Amino Acid Repeats From Trypanosoma cruzi Shed Antigens
Increase the Half-Life of Proteins in Blood
Carlos A. Buscaglia,
Julieta Alfonso,
Oscar Campetella, and
Alberto C.C. Frasch
From the Instituto de Investigaciones Biotecnológicas,
Universidad Nacional de General San Martín, Buenos Aires,
Argentina.
Proteins containing amino acid repeats are widespread among
protozoan parasites. It has been suggested that these repetitive structures act as immunomodulators, but other functional aspects may be
of primary importance. We have recently suggested that tandem repeats
present in Trypanosoma cruzi trans-sialidase stabilize the
catalytic activity in blood. Because the parasite releases trans-sialidase, this delayed clearance of the enzyme might
have implications in vivo. In the present work, the ability of
repetitive units from different T. cruzi molecules in
stabilizing trans-sialidase activity in blood was
evaluated. It is shown that repeats present on T. cruzi shed
proteins (antigens 13 and Shed-Acute-Phase-Antigen [SAPA])
increase trans-sialidase half-life in blood from 7 to almost 35 hours. Conversely, those repeats present in intracellular T. cruzi proteins only increase the enzyme half-life in blood up to 15 hours. Despite these results, comparative analysis of structural and
catalytic properties of both groups of chimeric enzymes show no
substantial differences. Interestingly, antigens 13 and SAPA also
increase the persistence in blood of chimeric glutathione
S-transferases, thus suggesting that this effect is inherent to these
repeats and independent of the carrier protein. Although the molecular
basis of this phenomenon is still uncertain, its biotechnological
potential can be envisaged.
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