The topological structure and function of Echinococcus granulosus lactate dehydrogenase, a tegumental transmembrane protein

Gan, Wenjia; Zhang, Zhaoping; Li, Gang; Xu, Hongxu; Zeng, Suxiang; Li, Yuzhe; Wu, Wei; Hu, Xuchu

doi:10.1016/j.molbiopara.2012.04.004

Cited by 7 publications

(4 citation statements)

References 23 publications

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“…Among these differentially expressed proteins, a set of proteins were associated with the tricarboxylic acid cycle (TCA), such as malate, succinate, oxoglutarate, pyruvate, and lactate dehydrogenases. Some studies have reported that malate and lactate dehydrogenases may be important therapeutic targets for invasive parasites because they play critical roles in the progression and development of parasitic diseases (23,24). These findings indicate that the TCA enzyme is widely expressed in the PSCs and adults, suggesting that carbohydrate metabolism might be the primary energy source during E. granulosus development, and that the key TCA enzymes might be important potential candidate targets for vaccines and novel drug research against CE.…”

Section: Discussionmentioning

confidence: 92%

Global profiling of the proteome, phosphoproteome, and N-glycoproteome of protoscoleces and adult worms of Echinococcus granulosus

Wang,

Jia,

et al. 2023

Front. Vet. Sci.

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IntroductionCystic echinococcosis (CE) is a chronic zoonosis caused by infection with the metacestode of the Echinococcus granulosus. A unique characteristic of E. granulosus protoscolex (PSC) is their ability to develop bidirectionally into an adult worm in the definitive host or a secondary hydatid cyst in the intermediate host. Furthermore, cestodes have a complex life cycle involving different developmental stages; however, the mechanisms underlying this development remain unknown. Several studies have demonstrated that certain matrix proteins undergo posttranslational modifications (PTMs), including phosphorylation and glycosylation, which have important regulatory effects on their functional properties.MethodsSystematic analyses of the proteome, phosphorylated modified proteome, and glycosylated modified proteome of protoscoleces (PSCs) and adult worms were performed using a proteomic strategy. Data are available via ProteomeXchange with identifier PXD043166.ResultsIn total, 6,407 phosphorylation sites and 1757 proteins were quantified. Of these, 2032 phosphorylation sites and 770 proteins were upregulated, and 2,993 phosphorylation sites and 1,217 proteins were downregulated in adult worms compared to PSCs. A total of 612 N-glycosylation sites were identified in the 392 N-glycoproteins. Of these, 355 N-glycosylation sites and 212 N-glycoproteins were quantified. Of these, 90 N-glycosylation sites and 64 N-glycoproteins were upregulated, and 171 N-glycosylation sites and 126 N-glycoproteins were downregulated in adult worms compared to PSCs. GO enrichment analysis indicated that the differentially expressed phosphoproteins were mainly enriched in the regulation of oxidoreduction coenzyme metabolic processes, myelin sheath, and RNA helicase activity, whereas the differentially expressed N-glycoproteins were enriched in the cellular response to unfolded proteins, endoplasmic reticulum lumen, and nucleic acid binding. KEGG enrichment analysis indicated that the differently expressed phosphoproteins were mainly enriched in RNA transport, hypertrophic cardiomyopathy (HCM), glycolysis/gluconeogenesis, HIF-1 signaling pathway and pyruvate metabolism. Differentially expressed N-glycoproteins were enriched in the PI3K-Akt signaling pathway, ECM-receptor interactions, and protein processing in the endoplasmic reticulum.DiscussionTo our knowledge, this study is the first global phosphoproteomic and N-glycoproteomic analysis of E. granulosus, which provides valuable information on the expression characteristics of E. granulosus and provides a new perspective to elucidate the role of protein phosphorylation and N-glycosylation in the development of E. granulosus.

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Section: Discussionmentioning

confidence: 92%

Global profiling of the proteome, phosphoproteome, and N-glycoproteome of protoscoleces and adult worms of Echinococcus granulosus

Wang,

Jia,

et al. 2023

Front. Vet. Sci.

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“…Babesia LDH was localized on the cell membrane of infected erythrocytes [30]. Gan et al [14]. expressed four antigenic epitopes of Echinococcus granulosus LDH (EgLDH) and obtained antibodies against each epitope.…”

Section: Discussionmentioning

confidence: 99%

“…In addition, LDHs have been proven to be good diagnostic molecules and potential anthelminthic drug targets or vaccines [12]. Owing to the important functions and roles of LDH, a series of studies have been conducted on this enzyme in different tapeworms [13,14].…”

Section: Introductionmentioning

confidence: 99%

Lactate Dehydrogenase Gene Family in Spirometra mansoni (Cestoda: Diphyllobothriidea)—Phylogenetic Patterns and Molecular Characteristics

Liu,

Zhou,

Gao

et al. 2023

Animals

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The plerocercoid of Spirometra mansoni can parasitize both human and animals, resulting in sparganosis. Lactate dehydrogenase (LDH) is an important enzyme in parasites. However, our knowledge of the LDH family in S. mansoni is still inadequate. This work identified 19 new LDH members in S. mansoni. Clustering analysis demonstrated that all SmLDHs were divided into two main groups, which is consistent with the patterns of conserved motif organization. According to RT-qPCR, 2 LDHs were highly expressed in the plerocercoid stage and 17 LDHs were highly expressed in the adult stage. The evolutionary tree showed a high level of diversity of both cestode and trematode LDHs. SmLDHs contained both conserved family members and members in the process of further diversification. rSmLDH has a NAD-binding domain and a substrate-binding domain. The protein was immunolocalized in the epidermis of the pleroceroid and in the tegument, uterus and egg shell of adult worms. The optimum activity for rSmLDH in the pyruvate reduction reaction was found to be pH 4.5 and 37 °C. In the oxidation reaction, optimal values for pH and temperature were 9.0 and 30 °C, respectively. Gossypol was found to be the most powerful inhibitor in both reduction and oxidation reactions. The results provide a basis for the further study of the biological roles of LDHs in S. mansoni and other LDH-containing taxa.

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“…Study of E . granulosus LDH revealed that the linear B-cell epitopes aa 101–107, 191–196, and 307–313 related to the function of the LDH, and that LDH was a potential anti- E. granulosus drug target (Gan et al 2012 ). Further, Du et al ( 2011 ) analyzed the linear B-cell epitopes of TsLDH-A and TsLDH-B and discovered that cestodes have a common, specific epitope, which means LDH is a potential antiparasitic drug target (Du et al 2011 ).…”

Section: Discussionmentioning

confidence: 99%

Molecular cloing and bioinformatics analysis of lactate dehydrogenase from Taenia multiceps

et al. 2017

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Coenurus cerebralis, the larval stage (metacestode or coenurus) of Taenia multiceps, parasitizes sheep, goats, and other ruminants and causes coenurosis. In this study, we isolated and characterized complementary DNAs that encode lactate dehydrogenase A (Tm-LDHA) and B (Tm-LDHB) from the transcriptome of T. multiceps and expressed recombinant Tm-LDHB (rTm-LDHB) in Escherichia coli. Bioinformatic analysis showed that both Tm-LDH genes (LDHA and LDHB) contain a 996-bp open reading frame and encode a protein of 331 amino acids. After determination of the immunogenicity of the recombinant Tm-LDHB, an indirect enzyme-linked immunosorbent assay (ELISA) was developed for preliminary evaluation of the serodiagnostic potential of rTm-LDHB in goats. However, the rTm-LDHB-based indirect ELISA developed here exhibited specificity of only 71.42% (10/14) and sensitivity of 1:3200 in detection of goats infected with T. multiceps in the field. This study is the first to describe LDHA and LDHB of T. multiceps; meanwhile, our results indicate that rTm-LDHB is not a specific antigen candidate for immunodiagnosis of T. multiceps infection in goats.

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The topological structure and function of Echinococcus granulosus lactate dehydrogenase, a tegumental transmembrane protein

Cited by 7 publications

References 23 publications

Global profiling of the proteome, phosphoproteome, and N-glycoproteome of protoscoleces and adult worms of Echinococcus granulosus

Global profiling of the proteome, phosphoproteome, and N-glycoproteome of protoscoleces and adult worms of Echinococcus granulosus

Lactate Dehydrogenase Gene Family in Spirometra mansoni (Cestoda: Diphyllobothriidea)—Phylogenetic Patterns and Molecular Characteristics

Molecular cloing and bioinformatics analysis of lactate dehydrogenase from Taenia multiceps

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