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Identification of new sphingomyelinases D in pathogenic fungi and other pathogenic organisms.

Dias-Lopes C, Neshich IA, Neshich G, Ortega JM, Granier C, Chávez-Olortegui C, Molina F, Felicori L - PLoS ONE (2013)

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Departamento de Bioquímica-Imunologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Belo Horizonte, MG, Brazil.

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.

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Organisms with SMase D-like proteins.Metazoa (A), bacteria (B) and fungi (C). The species in gray have been described as possessing SMase D activities in previous works and, in blue, are the new species with SMase D-like proteins found in this work.
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pone-0079240-g001: Organisms with SMase D-like proteins.Metazoa (A), bacteria (B) and fungi (C). The species in gray have been described as possessing SMase D activities in previous works and, in blue, are the new species with SMase D-like proteins found in this work.

Mentions: Bidirectional best hits (BBH) analyses were performed to identify candidate SMase D enzymes in different species. This strategy was able to identify SMase D-like sequences in 24 distinct genera, 59 species and 105 subspecies upon extended searches in different databases such as NCBI nr, WGS, dbEST and TSA. In addition, the incomplete sequence of the Acari from the genera Dermatophagoides, Varroa, Psoroptes and Tetranychus were identified as possible SMase D-like proteins (data not shown). As shown in Figure 1, a significant variety of fungi ((Figure 1C, 11 genera) contain SMase D-like sequences compared to bacteria (Figure 1B), spiders and Acari (Figure 1A) (5, 4 and 4 genera, respectively). The majority of these sequences have never before been identified in silico or in vitro. For the 5 bacterial genera found, 3 were new: Burkholderia, Streptomyces and Austwickia (Figure 1 B, blue squares). Surprisingly, from the Sicariidae family, 2 new spider genera were also found: Acanthoscurria and Stegodyphus (Figure 1A), in which SMase D occurrence has never been reported until now. The searches identified SMase D similar sequences in 3 different Acari genera besides Ixodes scapularis (Figure 1A), where SMase D activity has been previously reported [9]. The novel Acari genera found were: Amblyomma, Rhipicephalus and Metaseiulus. In regards to fungi, the genera found were: Ajellomyces or Histoplasma, Arthroderma, Trichophyton, Uncinocarpus, Coccidioides, Paracoccidioides, Aspergillus, Gibberella, Fusarium, Metarrhizium and Passalora. The complete list of species, as well as the database source of SMase D-like sequences, is shown in Tables S1, S2 and S3.


Identification of new sphingomyelinases D in pathogenic fungi and other pathogenic organisms.

Dias-Lopes C, Neshich IA, Neshich G, Ortega JM, Granier C, Chávez-Olortegui C, Molina F, Felicori L - PLoS ONE (2013)

Organisms with SMase D-like proteins.Metazoa (A), bacteria (B) and fungi (C). The species in gray have been described as possessing SMase D activities in previous works and, in blue, are the new species with SMase D-like proteins found in this work.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3815110&req=5

pone-0079240-g001: Organisms with SMase D-like proteins.Metazoa (A), bacteria (B) and fungi (C). The species in gray have been described as possessing SMase D activities in previous works and, in blue, are the new species with SMase D-like proteins found in this work.
Mentions: Bidirectional best hits (BBH) analyses were performed to identify candidate SMase D enzymes in different species. This strategy was able to identify SMase D-like sequences in 24 distinct genera, 59 species and 105 subspecies upon extended searches in different databases such as NCBI nr, WGS, dbEST and TSA. In addition, the incomplete sequence of the Acari from the genera Dermatophagoides, Varroa, Psoroptes and Tetranychus were identified as possible SMase D-like proteins (data not shown). As shown in Figure 1, a significant variety of fungi ((Figure 1C, 11 genera) contain SMase D-like sequences compared to bacteria (Figure 1B), spiders and Acari (Figure 1A) (5, 4 and 4 genera, respectively). The majority of these sequences have never before been identified in silico or in vitro. For the 5 bacterial genera found, 3 were new: Burkholderia, Streptomyces and Austwickia (Figure 1 B, blue squares). Surprisingly, from the Sicariidae family, 2 new spider genera were also found: Acanthoscurria and Stegodyphus (Figure 1A), in which SMase D occurrence has never been reported until now. The searches identified SMase D similar sequences in 3 different Acari genera besides Ixodes scapularis (Figure 1A), where SMase D activity has been previously reported [9]. The novel Acari genera found were: Amblyomma, Rhipicephalus and Metaseiulus. In regards to fungi, the genera found were: Ajellomyces or Histoplasma, Arthroderma, Trichophyton, Uncinocarpus, Coccidioides, Paracoccidioides, Aspergillus, Gibberella, Fusarium, Metarrhizium and Passalora. The complete list of species, as well as the database source of SMase D-like sequences, is shown in Tables S1, S2 and S3.

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Departamento de Bioquímica-Imunologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Belo Horizonte, MG, Brazil.

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.

Show MeSH
Related in: MedlinePlus