Fructose-bisphosphate aldolase and enolase from Echinococcus granulosus: Genes, expression patterns and protein interactions of two potential moonlighting proteins

Autor: Henrique Bunselmeyer Ferreira, Norbel Galanti, Karina Mariante Monteiro, Karina Rodrigues Lorenzatto, Gabriela Prado Paludo, Rodolfo Paredes, Arnaldo Zaha, Marbella Maria Fonseca
Rok vydání: 2012
Předmět:
Models
Molecular
Moonlighting functions
Protein moonlighting
In silico
Molecular Sequence Data
030231 tropical medicine
Enolase
Fructose-bisphosphate aldolase
Echinococcus multilocularis
Host-Parasite Interactions
03 medical and health sciences
0302 clinical medicine
Species Specificity
Echinococcosis
Fructose-Bisphosphate Aldolase
Protein Interaction Mapping
parasitic diseases
Genetics
Animals
Glycolytic enzymes
Amino Acid Sequence
Echinococcus granulosus
Gene
Genes
Helminth
030304 developmental biology
0303 health sciences
Base Sequence
Sequence Homology
Amino Acid
biology
Gene Expression Profiling
Aldolase A
Helminth Proteins
General Medicine
DNA
Helminth
biology.organism_classification
Recombinant Proteins
3. Good health
Isoenzymes
Biochemistry
Phosphopyruvate Hydratase
biology.protein
Cestode
Host–parasite interplay
Zdroj: GENE
Artículos CONICYT
CONICYT Chile
instacron:CONICYT
ISSN: 0378-1119
DOI: 10.1016/j.gene.2012.06.046
Popis: Glycolytic enzymes, such as fructose-bisphosphate aldolase (FBA) and enolase, have been described as complex multifunctional proteins that may perform non-glycolytic moonlighting functions, but little is known about such functions, especially in parasites. We have carried out in silico genomic searches in order to identify FBA and enolase coding sequences in Echinococcus granulosus, the causative agent of cystic hydatid disease. Four FBA genes and 3 enolase genes were found, and their sequences and exon–intron structures were characterized and compared to those of their orthologs in Echinococcus multilocularis, the causative agent of alveolar hydatid disease. To gather evidence of possible non-glycolytic functions, the expression profile of FBA and enolase isoforms detected in the E. granulosus pathogenic larval form (hydatid cyst) (EgFBA1 and EgEno1) was assessed. Using specific antibodies, EgFBA1 and EgEno1 were detected in protoscolex and germinal layer cells, as expected, but they were also found in the hydatid fluid, which contains parasite's excretory–secretory (ES) products. Besides, both proteins were found in protoscolex tegument and in vitro ES products, further suggesting possible non-glycolytic functions in the host–parasite interface. EgFBA1 modeled 3D structure predicted a F-actin binding site, and the ability of EgFBA1 to bind actin was confirmed experimentally, which was taken as an additional evidence of FBA multifunctionality in E. granulosus. Overall, our results represent the first experimental evidences of alternative functions performed by glycolytic enzymes in E. granulosus and provide relevant information for the understanding of their roles in host–parasite interplay.
Databáze: OpenAIRE
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