STRUCTURAL and FUNCTIONAL-PROPERTIES of TRYPANOSOMA TRANS-SIALIDASE
dc.contributor.author | Schenkman, S. [UNIFESP] | |
dc.contributor.author | Eichinger, D. | |
dc.contributor.author | Pereira, MEA | |
dc.contributor.author | Nussenzweig, V | |
dc.contributor.institution | NYU | |
dc.contributor.institution | TUFTS UNIV | |
dc.contributor.institution | Universidade Federal de São Paulo (UNIFESP) | |
dc.date.accessioned | 2016-01-24T11:40:16Z | |
dc.date.available | 2016-01-24T11:40:16Z | |
dc.date.issued | 1994-01-01 | |
dc.description.abstract | Sialic acids and sialidases play important roles in cellular interactions and modulate the recognition of pathogenic microbes by mammalian host cells. Protozoan parasites of the genus Trypanosoma express a unique sialic acid metabolizing enzyme. This enzyme, named trans-sialidase (TS), catalyzes the transfer of sialic acids from host glycoconjugates to acceptor molecules of the parasite plasma membrane. in African trypanosomes, the agents of sleeping sickness, TS is found only in forms developing within the insect vector, and the enzyme sialylates the major surface protein. in Trypanosoma cruzi, the causative agent of Chagas' disease in Central and South America, TS is expressed both in the insect and mammalian forms of the parasite. the T. cruzi enzyme has been biochemically characterized, and the gene encoding the enzyme has been cloned. the enzyme sialylates abundant mucin-like molecules present on the surface of the parasite. Several lines of evidence suggest that TS and sialic acid accepters on the surface of T. cruzi participate in host-parasite interactions and mediate the initial stages of the trypanosomes' invasion of host cells. | en |
dc.description.affiliation | NYU,MED CTR,DEPT PATHOL,MICHAEL HEIDELBERGER DIV IMMUNOL,NEW YORK,NY 10016 | |
dc.description.affiliation | TUFTS UNIV,NEW ENGLAND MED CTR HOSP,DEPT MED,DIV GEOG MED & INFECT DIS,BOSTON,MA 02111 | |
dc.description.affiliationUnifesp | Universidade Federal de São Paulo, EPM, Departamento de Microbiologia, Imunologia e Parasitologia, São Paulo, Brasil | |
dc.description.source | Web of Science | |
dc.format.extent | 499-523 | |
dc.identifier | http://dx.doi.org/10.1146/annurev.mi.48.100194.002435 | |
dc.identifier.citation | Annual Review of Microbiology. Palo Alto: Annual Reviews Inc, v. 48, p. 499-523, 1994. | |
dc.identifier.doi | 10.1146/annurev.mi.48.100194.002435 | |
dc.identifier.issn | 0066-4227 | |
dc.identifier.uri | http://repositorio.unifesp.br/handle/11600/25382 | |
dc.identifier.wos | WOS:A1994PM44600019 | |
dc.language.iso | eng | |
dc.publisher | Annual Reviews Inc | |
dc.relation.ispartof | Annual Review of Microbiology | |
dc.rights | info:eu-repo/semantics/restrictedAccess | |
dc.subject | SIALIC ACIDS | en |
dc.subject | CELL INVASION | en |
dc.subject | MUCIN | en |
dc.subject | SIALIDASE | en |
dc.subject | OLIGOSACCHARIDE SYNTHESIS | en |
dc.title | STRUCTURAL and FUNCTIONAL-PROPERTIES of TRYPANOSOMA TRANS-SIALIDASE | en |
dc.type | info:eu-repo/semantics/article |