title: Fructose-bisphosphate aldolase and enolase from Echinococcus granulosus: genes, expression patterns and protein interactions of two potential moonlighting proteins.
abstract: 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.
authors: Laboratório de Genômica Estrutural e Funcional and Laboratório de Biologia Molecular de Cestódeos, Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul, Porto Alegre, RS, Brazil.
authors: Karina Rodrigues
authors: KR
authors: Lorenzatto
authors: Karina Mariante
authors: KM
authors: Monteiro
authors: Rodolfo
authors: R
authors: Paredes
authors: Gabriela Prado
authors: GP
authors: Paludo
authors: Marbella Maria
authors: MM
authors: da Fonsêca
authors: Norbel
authors: N
authors: Galanti
authors: Arnaldo
authors: A
authors: Zaha
authors: Henrique Bunselmeyer
authors: HB
authors: Ferreira
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D018509:DNA, Helminth / Q000235:genetics; D004443:Echinococcosis / Q000469:parasitology; D048209:Echinococcus granulosus / Q000201:enzymology* / Q000235:genetics* / Q000472:pathogenicity; D048210:Echinococcus multilocularis / Q000201:enzymology / Q000235:genetics; D005634:Fructose-Bisphosphate Aldolase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D020869:Gene Expression Profiling; D017238:Genes, Helminth; D015801:Helminth Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D006790:Host-Parasite Interactions; D007527:Isoenzymes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010751:Phosphopyruvate Hydratase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D025941:Protein Interaction Mapping; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity
chemical_list: D018509:DNA, Helminth; D015801:Helminth Proteins; D007527:Isoenzymes; D011994:Recombinant Proteins; D005634:Fructose-Bisphosphate Aldolase; D010751:Phosphopyruvate Hydratase