DEAD/DExH-Box RNA Helicases in Selected Human Parasites

Marchat, Laurence A.; Arzola-Rodríguez, Silvia I.; Cruz, Olga Hernandez-de la; López-Rosas, Itzel; López‐Camarillo, César

doi:10.3347/kjp.2015.53.5.583

Cited by 17 publications

(9 citation statements)

References 70 publications

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“…The N and C-terminal extensions help in recruitment of the other interacting protein partners to the complex responsible for the specific function inside the cell 25 . Helicases regulate major biological pathways such as genome replication, translation, repair, mRNA splicing and transcription in all the organisms including malaria parasite 26,27 . Furthermore, helicases are also involved in cross-talk with various other biological pathways such as autophagy, apoptosis and homeostasis regulations 28–30 .…”

Section: Introductionmentioning

confidence: 99%

Plasmodium falciparum specific helicase 2 is a dual, bipolar helicase and is crucial for parasite growth

Chauhan

Tuteja

2019

Sci Rep

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Human malaria infection is a major challenge across the globe and is responsible for millions of deaths annually. Rapidly emerging drug resistant strains against the new class of anti-malarial drugs are major threat to control the disease burden worldwide. Helicases are present in every organism and have important role in various nucleic acid metabolic processes. Previously we have reported the presence of three parasite specific helicases (PSH) in Plasmodium falciparum 3D7 strain. Here we present the detailed biochemical characterization of PfPSH2. PfPSH2 is DNA and RNA stimulated ATPase and is able to unwind partially duplex DNA and RNA substrates. It can translocate in both 3′ to 5′ and 5′ to 3′ directions. PfPSH2 is expressed in all the stages of intraerythrocytic development and it is localized in cytoplasm in P. falciparum 3D7 strain. The dsRNA mediated inhibition study suggests that PfPSH2 is important for the growth and survival of the parasite. This study presents the detailed characterization of PfPSH2 and lays the foundation for future development of PfPSH2 as drug target.

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Section: Introductionmentioning

confidence: 99%

Plasmodium falciparum specific helicase 2 is a dual, bipolar helicase and is crucial for parasite growth

Chauhan

Tuteja

2019

Sci Rep

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“…As predicted in silico , MEDLE proteins are characterized with the presence of domains for ATP-dependent RNA helicase, histone chaperone, and serine/threonine protein kinase. The former two are known to be involved in transcriptional regulations while the latter is well known to target immunity-related GTPases (IRGs) for host immunity evasion in Toxoplasma gondii [ 22 , 23 ]. Thus, in addition to regulating parasite gene transcription during parasite growth and development, the secretion of these proteins into host cells during invasion could modulate host gene expression and serve as an immune evasion mechanism.…”

Section: Discussionmentioning

confidence: 99%

Characterization of MEDLE-1, a protein in early development of Cryptosporidium parvum

Fei

et al. 2018

Parasites Vectors

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BackgroundCryptosporidium spp. are important diarrhea-causing pathogens in humans and animals. Comparative genomic analysis indicated that Cryptosporidium-specific MEDLE family proteins may contribute to host adaptation of Cryptosporidium spp., and a recent study of one member of this family, CpMEDLE-2 encoded by cgd5_4590, has provided evidence supporting this hypothesis. In this study, another member of the protein family, CpMEDLE-1 of Cryptosporidium parvum encoded by cgd5_4580, which is distinct from CpMEDLE-2 and has no signature motif MEDLE, was cloned, expressed and characterized to understand its function.MethodsCpMEDLE-1 was expressed in Escherichia coli and polyclonal antibodies against the recombinant CpMEDLE-1 protein were prepared in rabbits. Quantitative PCR was used to analyze the expression profile of cgd5_4580 in C. parvum culture. Immunofluorescence staining was used to locate CpMEDLE-1 expression in life-cycle stages, and in vitro neutralization assay with antibodies was adopted to assess the role of the protein in C. parvum invasion.ResultsThe results indicated that cgd5_4580 had a peak expression at 2 h of C. parvum culture. CpMEDLE-1 was located in the mid-anterior region of sporozoites, probably within the dense granules. The neutralization efficiency of anti-CpMEDLE-1 antibodies was approximately 40%.ConclusionsThe differences in protein and gene expression profiles between CpMEDLE-1 and CpMEDLE-2 suggest that MEDLE proteins have different subcellular locations, are developmentally regulated, could be potentially involved in the transcriptional regulation of the expression of parasite or host proteins and may exert their functions in different stages of the invasion and development process.

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“…SF2 contains 8-9 highly conserved motifs, including motifs Q, I, Ia, Ib, II, III, IV, V and VI, each of which display a distinct function. Motifs I, II, VI and Q bind to NTP and catalyze hydrolysis; motifs Ia, Ib and IV primarily bind to RNA substrates; and motifs III and V connect the NTP binding and RNA recognition sites, promoting NTP-dependent RNA unwinding (6,7). Based on the amino acid sequence of conserved motif II,…”

Section: Introductionmentioning

confidence: 99%

Structure and function of DEAH-box helicase 32 and its role in cancer (Review)

et al. 2021

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DEAH-box helicase 32 (DHX32) is an RNA helicase with unique structural characteristics that is involved in numerous biological processes associated with RNA, including ribosome biosynthesis, transcription, mRNA splicing and translation. Increasing evidence suggests that abnormal DHX32 expression contributes to cancer initiation and development, due to dysregulated cell proliferation, differentiation, apoptosis and other processes. In the current review, the discovery, structure and function of DHX32, as well as the association between abnormal DHX32 expression and tumors are discussed. DHX32 expression is downregulated in acute lymphoblastic leukemia, but upregulated in solid tumors, including colorectal and breast cancer. Furthermore, DHX32 expression levels are associated with the pathological and clinical features of the cancer. Therefore, DHX32 may serve as a novel liquid biopsy marker for auxiliary diagnosis and prognosis screening, as well as a possible target for cancer therapy. The molecular mechanism underlying the contribution of DHX32 towards the initiation and development of cancer requires further investigation for the development of anticancer treatments based on manipulating DHX32 expression and function.

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DEAD/DExH-Box RNA Helicases in Selected Human Parasites

Cited by 17 publications

References 70 publications

Plasmodium falciparum specific helicase 2 is a dual, bipolar helicase and is crucial for parasite growth

Plasmodium falciparum specific helicase 2 is a dual, bipolar helicase and is crucial for parasite growth

Characterization of MEDLE-1, a protein in early development of Cryptosporidium parvum

Structure and function of DEAH-box helicase 32 and its role in cancer (Review)

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