Article
Substrate specificity of the Trypanosoma cruzi trans-sialidase
Registro en:
VANDEKERCKHOVE, F. et al. Substrate specificity of the Trypanosoma cruzi trans-sialidase. Glycobiology, v. 2, n. 6, p. 541-548, 1992.
0959-6658
Autor
Vandekerckhove, Filip
Schenkman, Sergio
Pontes-de-Carvalho, Lain Carlos
Tomlinson, Stephen
Kiso, Makoto
Yoshida, Masahiro
Hasegawa, Akira
Nussenzweig, Victor
Resumen
Pontes-de-Carvalho, Lain Carlos. Fundação Oswaldo Cruz. Instituto Gonçalo Moniz. Salvador, BA, Brasil. “Documento produzido em parceria ou por autor vinculado à Fiocruz, mas não consta à informação no documento”. MacArthur Foundation, the UNDP/World
Bank/WHO Special Program for Research and Training in Tropical Diseases,
Conselho Nacional de Desenvolvimento Cientifico e Tecnologico and Fundacao
de Amparo a Pesquisa do Estado de Sao Paulo (Brazil) F.V. is a Research
Assistant of the Belgian National Fund for Scientific Research (NFWO), L.P.C
is a recipient of a grant from the Secretana de Ciencia e Tecnologia (Programa
RHAE), Brazil. Trypanosoma cruzi trypomastigotes acquire sialic acid (SA)
from host glycoconjugates by means of a plasma membraneassociated
trans-sialidase (TS). Here we study the substrate
specificity of TS, which differs from all known sialyltransferases
in that it does not require cytidine monophosphate
(CMD-SA as donor. The T.cruzi TS reversibly
transfers SA to saccharides with terminal /3-Gal (but not
a-Gal) residues. Donors are saccharides with SA linked to
terminal /3-Gal residues by (a2-3), but not (a2-6) bonds. The
type of /3-linkage of the terminal Gal residue is of minor
importance (/31-4 and 01-6 are slightly better than /Sl-3),
whereas chain length and the structure of additional vicinal
sugar residues are not relevant. SA on the surface of living
trypomastigotes of T. cruzi is transferred back and forth
between the parasite surface and acceptor molecules with
terminal /3-Gal, either in solution or on the surface of
neighbouring mammalian cells. Addition of fucose residue
on or close to the terminal galactose impairs TS activity. As
a consequence, the enzyme acts poorly on the E-selectin
ligand sialyl-Lewis" and its precursor Lewis1, and in vitro
adhesion of TS-treated neutrophils to L-cells expressing
L-selectin is not affected. Modifications in the structure of
the (a2-3)-linked iV-acetyl-neuraminic acid (Neu5Ac) (deoxy
or methoxv) of the donor molecules do not impair transfer
if the changes are at C9, whereas changes at C4, C7 and C8
impair the ability to donate the modified SA. Compounds
with modified C4 and C8 inhibit TS at relatively high
inhibitor/substrate ratios.
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