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A PROTEOLYTIC FRAGMENT OF TRYPANOSOMA CRUZI TRANS-SIALIDASE LACKING THE CARBOXYL-TERMINAL DOMAIN IS ACTIVE, MONOMERIC, AND GENERATES ANTIBODIES THAT INHIBIT ENZYMATIC ACTIVITY
Affilliation
Escola Paulista de Medicina. Department of Microbiology, Immunology and Parasitology. São Paulo, SP, Brazil
Escola Paulista de Medicina. Department of Microbiology, Immunology and Parasitology. São Paulo, SP, Brazil
New York University Medical Center. Michael Heidelberger Division of Immunology. New York, New York
New York University Medical Center. Michael Heidelberger Division of Immunology. New York, New York
Escola Paulista de Medicina. Department of Microbiology, Immunology and Parasitology. São Paulo, SP, Brazil
New York University Medical Center. Michael Heidelberger Division of Immunology. New York, New York
New York University Medical Center. Michael Heidelberger Division of Immunology. New York, New York
Abstract
trans-Sialidase isolated from trypomastigote forms of
IlZypanosoma cruzi, the protozoan parasite that causes
Chagas’ disease, is multimeric and heterogeneous in
size. We show here that limited proteolysis of trans-sialidase
with papain yields a single monomeric polypeptide
chain of 70 kDa that conserves full enzymatic activity on
soluble and membrane-bound substrates. The papain
fragment lacks most otfh e 12-amino acid repeats of the
carboxyl-terminal domain that comprises about 50% of
the native trans-sialidase. When injected into rabbits,
the papain-generated fragmenitn duces antibodies that
inhibit trans-sialidase activity and trypomastigote sialylation.
The repeats are also not required for the stability
of the enzyme or fotrh e correct folding during the
biosynthesis in Escherichia coli, but seem essential for
trans-sialidase oligomerization. We conclude that transsialidase
is composed of two structurally and functionally
independent domains.
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