Mostrar el registro sencillo del ítem
Autor | Fonseca, Leonardo Marques da | |
Autor | Costa, Kelli Monteiro da | |
Autor | Chaves, Victoria de Sousa | |
Autor | Lima, Célio Geraldo Freire de | |
Autor | Morrot, Alexandre | |
Autor | Previato, Lucia Mendonça | |
Autor | Previato, Jose Osvaldo | |
Autor | Lima, Leonardo Freire de | |
Fecha de acceso | 2019-09-16T18:38:06Z | |
Fecha de disponibilización | 2019-09-16T18:38:06Z | |
Fecha de publicación | 2019 | |
Referencia | FONSECA, Leonardo Marques da et al. Theft and reception of host cell´s Sialic Acid: dynamics of Trypanosoma Cruzi Trans-sialidases and Mucin-Like Moleculares on Chagas` Diesease Immunomodulation. Frontiers in Immunology, v. 10, p. 1-10, Feb. 2019. | pt_BR |
ISSN | 1664-3224 | pt_BR |
URI | https://www.arca.fiocruz.br/handle/icict/35608 | |
Idioma | eng | pt_BR |
Editor | Frontiers Media | pt_BR |
Derechos de autor | open access | pt_BR |
Palabras clave en Portugués | Trypanosoma cruzi | pt_BR |
Palabras clave en Portugués | Ácido N-Acetilneuramínico | pt_BR |
Palabras clave en Portugués | Doença infecciosa | pt_BR |
Palabras clave en Portugués | Resposta da célula T | pt_BR |
Palabras clave en Portugués | Proteína de ligação à glicina | pt_BR |
Palabras clave en Portugués | Doença de Chagas | pt_BR |
Título | Theft and reception of host cell`s Sialic Acid: dynamics of Trypanosoma Cruzi Trans-sialidases and Mucin-Like molecules on Chagas´s Disease Immunomodulation | pt_BR |
Tipo del documento | Article | pt_BR |
DOI | 10.3389/fimmu.2019.00164 | |
Resumen en Inglés | The last decades have produced a plethora of evidence on the role of glycans, from cell adhesion to signaling pathways. Much of that information pertains to their role on the immune system and their importance on the surface of many human pathogens. A clear example of this is the flagellated protozoan Trypanosoma cruzi, which displays on its surface a great variety of glycoconjugates, including O-glycosylated mucin-like glycoproteins, as well as multiple glycan-binding proteins belonging to the trans-sialidase (TS)family.Amongthelatter,differentandconcurrentlyexpressedmoleculesmaypresent or not TS activity, and are accordingly known as active (aTS) and inactive (iTS) members. Over the last thirty years, it has been well described that T. cruzi is unable to synthesize sialic acid (SIA) on its own, making use of aTS to steal the host’s SIA. Although iTS did not show enzymatic activity, it retains a substrate specificity similar to aTS (α-2,3 SIA-containing glycotopes), displaying lectinic properties. It is accepted that aTS members act as virulence factors in mammals coursing the acute phase of the T. cruzi infection. However, recent findings have demonstrated that iTS may also play a pathogenic role during T. cruzi infection, since it modulates events related to adhesion and invasion of the parasite into the host cells. Since both aTS and iTS proteins share structural substrate specificity, it might be plausible to speculate that iTS proteins are able to assuage and/or attenuate biological phenomena depending on the catalytic activity displayed by aTS members. Since SIA-containing glycotopes modulate the host immune system, it should not come as any surprise that changes in the sialylation of parasite’s mucin-like molecules, as well as host cell glycoconjugates might disrupt critical physiological events, such as the building of effective immune responses. This review aims to discuss the importance of mucin-like glycoproteins and both aTS and iTS for T. cruzi biology, as well as to present a snapshot of how disturbances in both parasite and host cellsialoglycophenotypes may facilitatethe persistence of T. cruzi in the infected mammalian host. | pt_BR |
Afiliación | Universidade Federal do Rio de Janeiro. Instituto de Biofísica Carlos Chagas Filho. Laboratório de Glicobiologia. Rio de Janeiro, RJ, Brasil. | pt_BR |
Afiliación | Universidade Federal do Rio de Janeiro. Instituto de Biofísica Carlos Chagas Filho. Laboratório de Glicobiologia. Rio de Janeiro, RJ, Brasil. | pt_BR |
Afiliación | Universidade Federal do Rio de Janeiro. Instituto de Biofísica Carlos Chagas Filho. Laboratório de Glicobiologia. Rio de Janeiro, RJ, Brasil. | pt_BR |
Afiliación | Universidade Federal do Rio de Janeiro. Instituto de Biofísica Carlos Chagas Filho. Laboratório de Imunomodulação. Rio de Janeiro, RJ, Brasil. | pt_BR |
Afiliación | Universidade Federal do Rio de Janeiro. Faculdade de Medicina. Laboratório de Pesquisa em Tuberculose. Rio de Janeiro, RJ, Brasil / Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Imunoparasitologia. Rio de Janeiro, RJ, Brasil. | pt_BR |
Afiliación | Universidade Federal do Rio de Janeiro. Instituto de Biofísica Carlos Chagas Filho. Laboratório de Glicobiologia. Rio de Janeiro, RJ, Brasil. | pt_BR |
Afiliación | Universidade Federal do Rio de Janeiro. Instituto de Biofísica Carlos Chagas Filho. Laboratório de Glicobiologia. Rio de Janeiro, RJ, Brasil. | pt_BR |
Afiliación | Universidade Federal do Rio de Janeiro. Instituto de Biofísica Carlos Chagas Filho. Laboratório de Glicobiologia. Rio de Janeiro, RJ, Brasil. | pt_BR |
Palavras clave en Inglês | Trypanosoma cruzi | pt_BR |
Palavras clave en Inglês | Trans-sialidase | pt_BR |
Palavras clave en Inglês | Mucin-like molecule | pt_BR |
Palavras clave en Inglês | Sialic acid | pt_BR |
Palavras clave en Inglês | Glycan-binding protein | pt_BR |
Palavras clave en Inglês | Infectious disease | pt_BR |
Palavras clave en Inglês | T-cell response | pt_BR |
Palavras clave en Inglês | Chagas Disease | pt_BR |
DeCS | Ácido N-Acetilneuramínico | pt_BR |
DeCS | Mucina | pt_BR |
Ficheros en el ítem
Este ítem aparece en la(s) siguiente(s) colección(ones)
-
IOC - Artigos de Periódicos [12500]