Data/hora: 23/06/2024 20:31:08

Biblioteca(s): | Embrapa Agricultura Digital.
Data corrente: | 02/01/2014
Data da última atualização: | 02/01/2014
Autoria: | DIAS-LOPES, C.; NESHICH, I. A. P.; NESHICH, G.; ORTEGA, J. M.; GRANIER, C.; CHÁVEZ-OLORTEGUI, C.; MOLINA, F.; FELICORI, L.
Afiliação: | CAMILA DIAS-LOPES, UFMG; IZABELLA A. P. NESHICH, Unicamp; GORAN NESHICH, CNPTIA; JOSÉ MIGUEL ORTEGA, UFMG; CLAUDE GRANIER, SysDiag UMR 3145 CNRS/BioRad; CARLOS CHÁVEZ-OLORTEGUI, UFMG; FRANCK MOLINA, SysDiag UMR 3145 CNRS/BioRad; LIZA FELICORI, UFMG.
Título: | Identification of new Sphingomyelinases D in pathogenic fungi and other pathogenic organisms.
Ano de publicação: | 2013
Fonte/Imprenta: | PLoS ONE, San Francisco, v. 8, n. 11, p. 1-12, 2013.
ISBN: | 10.1371/journal.pone.0079240
Idioma: | Inglês
Conteúdo: | Sphingomyelinases D (SMases D) or dermonecrotic toxins are well characterized in Loxosceles spider venoms and have been described in some strains of pathogenic microorganisms, such as Corynebacterium sp. After spider bites, the SMase D molecules cause skin necrosis and occasional severe systemic manifestations, such as acute renal failure. In this paper, we identified new SMase D amino acid sequences from various organisms belonging to 24 distinct genera, of which, 19 are new. These SMases D share a conserved active site and a C-terminal motif. We suggest that the C-terminal tail is responsible for stabilizing the entire internal structure of the SMase D Tim barrel and that it can be considered an SMase D hallmark in combination with the amino acid residues from the active site. Most of these enzyme sequences were discovered from fungi and the SMase D activity was experimentally confirmed in the fungus Aspergillus flavus. Because most of these novel SMases D are from organisms that are endowed with pathogenic properties similar to those evoked by these enzymes alone, they might be associated with their pathogenic mechanisms.
Palavras-Chave: | Bioinformática; Enzimas; Esfingomielinas.
Thesaurus Nal: | Bioinformatics; Enzymes; Sphingomyelins.
Categoria do assunto: | X Pesquisa, Tecnologia e Engenharia
URL: | http://ainfo.cnptia.embrapa.br/digital/bitstream/item/94633/1/Sphingomyelinases-D.pdf
Registro original: | Embrapa Agricultura Digital (CNPTIA)
Exemplares: | CNPTIA - (17704-1) - UPC - AP - DD -  -  -  - DIS