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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Identification of New Sphingomyelinases D in Pathogenic Fungi and Other Pathogenic Organisms

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Autor(es):
Dias-Lopes, Camila [1] ; Neshich, Izabella A. P. [2] ; Neshich, Goran [3] ; Ortega, Jose Miguel [1] ; Granier, Claude [4] ; Chavez-Olortegui, Carlos [1] ; Molina, Franck [4] ; Felicori, Liza [1]
Número total de Autores: 8
Afiliação do(s) autor(es):
[1] Univ Fed Minas Gerais, Inst Ciencias Biol, Dept Bioquim Imunol, Belo Horizonte, MG - Brazil
[2] Univ Estadual Campinas UNICAMP, Ctr Biol Mol & Engn Genet, Campinas, SP - Brazil
[3] Embrapa Informat Technol, Campinas, SP - Brazil
[4] BioRad, CNRS, SysDiag UMR 3145, Montpellier - France
Número total de Afiliações: 4
Tipo de documento: Artigo Científico
Fonte: PLoS One; v. 8, n. 11 NOV 1 2013.
Citações Web of Science: 11
Resumo

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. (AU)

Processo FAPESP: 12/00235-5 - Mecanismos de indução da via da sacaropina em células humanas
Beneficiário:Izabella Agostinho Pena
Modalidade de apoio: Bolsas no Brasil - Doutorado Direto
Processo FAPESP: 09/16376-4 - Aplicação de técnicas de reconhecimento de padrões usando os descritores estruturais de proteínas da base de dados do software STING para discriminação do sítio catalítico de enzimas
Beneficiário:Goran Nesic
Modalidade de apoio: Auxílio à Pesquisa - Regular