Complete NMR assignments for the second microneme adhesive repeat (MAR) domain from Eimeria tenella microneme protein EtMIC3

Lai, Livia; Simpson, Peter; Bumstead, Janine; Tomley, Fiona M.; Matthews, Stephen

doi:10.1007/s12104-009-9168-2

Cited by 11 publications

(11 citation statements)

References 8 publications

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“…Microneme proteins (MICs) are secreted from the parasite apex either singly or as protein complexes onto the parasite surface (Tomley et al ., 1996; Brown et al ., 2000; Bumstead and Tomley, 2000; Lai et al ., 2009) a process mediated in T. gondii by DOC2 proteins that recruit the necessary membrane-fusion machinery (Farrell et al ., 2012). ‘Capping’ models of motility, whereby parasite molecules are rapidly translocated backwards over the surface to promote forward motion, were proposed over 40 years ago for Plasmodium (circumsporozoite precipitation reaction, Vanderberg, 1974), Eimeria nieschulzi (capping of ferritin, Dubremetz and Torpier, 1978) and gregarines (capping of conA-coated latex beads, King, 1981).…”

Section: The Life Cycle Of Eimeria Speciesmentioning

confidence: 99%

Life cycle stages, specific organelles and invasion mechanisms ofEimeriaspecies

et al. 2019

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Apicomplexans, including species of Eimeria, pose a real threat to the health and wellbeing of animals and humans. Eimeria parasites do not infect humans but cause an important economic impact on livestock, in particular on the poultry industry. Despite its high prevalence and financial costs, little is known about the cell biology of these ‘cosmopolitan’ parasites found all over the world. In this review, we discuss different aspects of the life cycle and stages of Eimeria species, focusing on cellular structures and organelles typical of the coccidian family as well as genus-specific features, complementing some ‘unknowns’ with what is described in the closely related coccidian Toxoplasma gondii.

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Section: The Life Cycle Of Eimeria Speciesmentioning

confidence: 99%

Life cycle stages, specific organelles and invasion mechanisms ofEimeriaspecies

et al. 2019

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“…However, to date all MAR domains identified in Eimeria species are exclusively Type I, suggesting that a lack of Type II MAR may contribute to the exquisite host and site specificity displayed by these parasites [ 21 , 22 ]. For Eimeria tenella , EtMIC3 containing seven Type I MAR binds a restricted range of sialyl glycans with a strong preference for ɑ2,3-linkages that are predominant in the chicken gut [ 22 , 23 ]. Four additional Type I MAR containing proteins (EtMCP2 with 1 MAR; EtMCP3 with 3 MAR; EtMCP4 with 4 MAR, EtMCP5 with 2 MAR) are present in the E. tenella genome [ 21 ] (Table 1 ) but their subcellular location, stage-expression and function are unknown.…”

Section: Introductionmentioning

confidence: 99%

Characterization of novel microneme adhesive repeats (MAR) in Eimeria tenella

et al. 2017

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BackgroundThe phylum Apicomplexa comprises a wide variety of parasites of significant medical and economic relevance. These parasites have extremely different host and tissue tropisms; for example Toxoplasma gondii can invade virtually any nucleated cell and infect almost all warm-blooded vertebrates, whereas Eimeria tenella infects only chickens and is restricted in its growth to epithelial cells of the caecum. Proteins released from the microneme secretory organelles (MICs) are critical for apicomplexan invasion of host cells and allow parasites to bind a diverse range of host cell oligosaccharide epitopes. MICs bear modular arrangements of sequences with adhesive proteins and interestingly the sialic-acid binding MAR (microneme adhesive repeat) domain containing proteins (MCPs) are suggested to make significant contributions to the different host and tissue tropisms of T. gondii and E. tenella.ResultsIn this study, we evaluated the binding capacity of Type I MAR domains from novel E. tenella MCPs. Variants of the previously described HxT motif were analysed showing that HxT and VxT variants bind, whereas HxS and YxE variants did not. One of these MCP containing a single MAR (EtMCP2) showed an apical localization when expressed as a fusion with the fluorescent reporter mCherry in transgenic populations and a similar pattern of transcripts per zoite during endogenous development in vitro as the well-characterised microneme protein EtMIC2.ConclusionsVariation in the binding properties of the MAR of different EtMCPs was confirmed and their ability to bind a wider range of sialic acids and terminal linkages should be studied. In addition, transgenesis technology has been used for first time in Eimeria parasites as a rapid tool for the study of endogenous protein localization by fusion with a fluorescent reporter.Electronic supplementary materialThe online version of this article (10.1186/s13071-017-2454-4) contains supplementary material, which is available to authorized users.

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“…Microneme proteins are a unique group of secreted proteins peculiar to the parasites belonging to the phylum Apicomplexa including Eimeria , which are mainly involved in the process of parasite adhesion and invasion of the host cells [ 29 , 30 ]. In the early stages of parasite interaction with the host cells, microneme proteins are first secreted from the apex of the merozoite and promote the adhesion by recognizing the receptors on the host cell membrane, thus making them crucial contributors to the invasion process of parasites [ 31 ]. Due to these features, previous studies have mainly focused on microneme proteins as recombinant diagnostic antigens, vaccine candidate antigens, and anti-parasitic drug targets in the control of several apicomplexan parasite infections, including Toxoplasma gondii [ 32 , 33 , 34 ], Plasmodium falciparum [ 35 , 36 ], Neospora caninum [ 37 , 38 ], and Eimeria tenella [ 39 , 40 , 41 ].…”

Section: Discussionmentioning

confidence: 99%

Expression Analysis and Serodiagnostic Potential of Microneme Proteins 1 and 3 in Eimeria stiedai

Wei

Shen

Xiao

et al. 2020

Genes

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Eimeria stiedai is an apicomplexan protozoan parasite that invades the liver and bile duct epithelial cells in rabbits and causes severe hepatic coccidiosis, resulting in significant economic losses in the domestic rabbit industry. Hepatic coccidiosis lacks the typical clinical symptoms and there is a lack of effective premortem tools to timely diagnose this disease. Therefore, in the present study we cloned and expressed the two microneme proteins i.e., microneme protein 1 (EsMIC1) and microneme protein 3 (EsMIC3) from E. stiedai and used them as recombinant antigens to develop a serodiagnostic method for an effective diagnosis of hepatic coccidiosis. The cDNAs encoding EsMIC1 and EsMIC3 were cloned and the mRNA expression levels of these two genes at different developmental stages of E. stiedai were determined by quantitative real-time PCR analysis (qRT-PCR). The immunoreactivity of recombinant EsMIC1 (rEsMIC1) and EsMIC3 (rEsMIC3) proteins were detected by Western blotting, and indirect enzyme-linked immunosorbent assays (ELISAs) based on these two recombinant antigens were established to evaluate their serodiagnostic potential. Our results showed that the proteins encoded by the ORFs of EsMIC1 (711 bp) and EsMIC3 (891 bp) were approximately 25.89 and 32.39 kDa in predicted molecular weight, respectively. Both EsMIC1 and EsMIC3 showed the highest mRNA expression levels in the merozoites stage of E. stiedai. Western blotting analysis revealed that both recombinant proteins were recognized by E. stiedai positive sera, and the indirect ELISAs using rEsMIC1 and rEsMIC3 were developed based on their good immunoreactivity, with 100% (48/48) sensitivity and 97.9% (47/48) specificity for rEsMIC1 with 100% (48/48) sensitivity and 100% (48/48) specificity for rEsMIC3, respectively. Moreover, rEsMIC1- and rEsMIC3-based indirect ELISA were able to detect corresponding antibodies in sera at days 6, 8, and 10 post E. stiedai infection, with the highest positive diagnostic rate (62.5% (30/48) for rEsMIC1 and 66.7% (32/48) for rEsMIC3) observed at day 10 post infection. Therefore, both EsMIC1 and EsMIC3 can be used as potential serodiagnostic candidate antigens for hepatic coccidiosis caused by E. stiedai.

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Complete NMR assignments for the second microneme adhesive repeat (MAR) domain from Eimeria tenella microneme protein EtMIC3

Abstract: Eimeria tenella is the causative agent of coccidiosis in domestic chickens. We report the complete backbone and side chain NMR assignments for the second microneme adhesive repeat of the microneme protein 3 of E. tenella.

Cited by 11 publications

References 8 publications

Life cycle stages, specific organelles and invasion mechanisms ofEimeriaspecies

Life cycle stages, specific organelles and invasion mechanisms ofEimeriaspecies

Characterization of novel microneme adhesive repeats (MAR) in Eimeria tenella

Expression Analysis and Serodiagnostic Potential of Microneme Proteins 1 and 3 in Eimeria stiedai

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