TY - JOUR
T1 - A novel cell surface trans-sialidase of trypanosoma cruzi generates a stage-specific epitope required for invasion of mammalian cells
AU - Schenkman, Sergio
AU - Jiang, Man Shiow
AU - Hart, Gerald Warren
AU - Nussenzweig, Victor
PY - 1991/6/28
Y1 - 1991/6/28
N2 - When trypomastigotes of T. cruzi emerge from cells of the mammalian host, they contain little or no sialic acids on their surfaces. However, rapidly upon entering the circulation, they express a unique cell surface trans-sialidase activity. This enzyme specifically transfers α(2-3)-linked sialic acid from extrinsic host-derived macromolecules to parasite surface molecules, leading to the assembly of Ssp-3, a trypomastigote-specific epitope. The T. cruzi trans-sialidase does not utilize cytidine 5′ monophospho-N-acetylneuraminic acid as a donor substrate, but readily transfers sialic acid from exogenously supplied α(2-3)-sialyllactose. Monoclonal antibodies that recognize sialic acid residues of Ssp-3 inhibit attachment of trypomastigotes to host cells, suggesting that the unusual trans-sialidase provides Ssp-3 with structural features required for target cell recognition.
AB - When trypomastigotes of T. cruzi emerge from cells of the mammalian host, they contain little or no sialic acids on their surfaces. However, rapidly upon entering the circulation, they express a unique cell surface trans-sialidase activity. This enzyme specifically transfers α(2-3)-linked sialic acid from extrinsic host-derived macromolecules to parasite surface molecules, leading to the assembly of Ssp-3, a trypomastigote-specific epitope. The T. cruzi trans-sialidase does not utilize cytidine 5′ monophospho-N-acetylneuraminic acid as a donor substrate, but readily transfers sialic acid from exogenously supplied α(2-3)-sialyllactose. Monoclonal antibodies that recognize sialic acid residues of Ssp-3 inhibit attachment of trypomastigotes to host cells, suggesting that the unusual trans-sialidase provides Ssp-3 with structural features required for target cell recognition.
UR - http://www.scopus.com/inward/record.url?scp=0025769326&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0025769326&partnerID=8YFLogxK
U2 - 10.1016/0092-8674(91)90008-M
DO - 10.1016/0092-8674(91)90008-M
M3 - Article
C2 - 1712251
AN - SCOPUS:0025769326
VL - 65
SP - 1117
EP - 1125
JO - Cell
JF - Cell
SN - 0092-8674
IS - 7
ER -