Advanced search
Start date
Betweenand
(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

Full text
Author(s):
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]
Total Authors: 8
Affiliation:
[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
Total Affiliations: 4
Document type: Journal article
Source: PLoS One; v. 8, n. 11 NOV 1 2013.
Web of Science Citations: 11
Abstract

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)

FAPESP's process: 12/00235-5 - Mechanisms of saccharopine pathway induction in human cells
Grantee:Izabella Agostinho Pena
Support type: Scholarships in Brazil - Doctorate (Direct)
FAPESP's process: 09/16376-4 - Prediction of catalytic site residues (CSR) for enzymes by applying pattern recognition on protein structural descriptors found in STING database
Grantee:Goran Nesic
Support type: Regular Research Grants