iTRAQ-based proteomic analysis reveals invasion-related proteins among three developmental stages of Eimeria necatrix

Gao, Yang; Suding, Zeyang; Wang, Lele; Liu, Dandan; Su, Shijie; Xu, Jing; Hu, Junjie; Tao, Jianping

doi:10.1016/j.jprot.2023.104939

Cited by 2 publications

(1 citation statement)

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“…Non-attenuated vaccines carry the potential risk of vaccine-induced disease. The high costs of attenuated vaccines limit their widespread use ( Gao et al., 2023 ). It is therefore essential to continue to research and develop innovative strategies to effectively control coccidiosis in poultry.…”

Section: Introductionmentioning

confidence: 99%

Localization in vivo and in vitro confirms EnApiAP2 protein encoded by ENH_00027130 as a nuclear protein in Eimeria necatrix

Cai,

Feng,

Wang

et al. 2023

Front. Cell. Infect. Microbiol.

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IntroductionApicomplexan AP2 family of proteins (ApiAP2) are transcription factors (TFs) that regulate parasite growth and development, but little is known about the ApiAP2 TFs in Eimeria spp. ENH_00027130 sequence is predicted to encode a Eimeria necatrix ApiAP2 protein (EnApiAP2).MethodsThe cDNAs encoding full-length and truncated EnApiAP2 protein were cloned and sequenced, respectively. Then, the two cDNAs were cloned into the pET28a(+) expression vector and expressed expressed in Escherichia coli BL21. The mouse polyclonal antibody (pAb) and monoclonal antibody (mAb) against recombinant EnApiAP2 (rEnApiAP2) and EnApiAP2tr (rEnApiAP2tr) were prepared and used to localize the native EnApiAP2 protein in E. necatrix, respectively. Finally, the recombinant pEGFP-C1-ΔNLS-EnApiAP2s (knockout of a nuclear localization sequence, NLS) and pEGFP-C1-EnApiAP2 plasmid were constructed and transfected into DF-1 cells, respectively, to further observe subcellular localization of EnApiAP2 protein.ResultsThe EnApiAP2 gene had a size of 5019 bp and encoded 1672 amino acids, containing a conserved AP2 domain with a secondary structure consisting of an α-helix and three antiparallel β-strands. The rEnApiAP2 and rEnApiAP2tr were predominantly expressed in the form of inclusion bodies, and could be recognized by the 6×His tag mAb and the serum of convalescent chickens after infection with E. necatrix, respectively. The native EnApiAP2 protein was detected in sporozoites (SZ) and second generation merozoites (MZ-2) extracts, with a size of approximately 210 kDa. A quantitative real-time PCR (qPCR) analysis showed that the transcription level of EnApiAP2 was significantly higher in SZ than in MZ-2, third generation merozoites (MZ-3) and gametocytes (P<0.01). EnApiAP2 protein was localized in the nuclei of SZ, MZ-2 and MZ-3 of E. necatrix. The protein of EnApiAP2 was localized in the nucleus of the DF-1 cells, whereas the ΔNLS-EnApiAP2 was expressed in the cytoplasm, which further confirmed that EnApiAP2 is nucleoprotein.DiscussionEnApiAP2 protein encoded by ENH_00027130 sequence was localized in the nucleus of E. necatrix parasites, and relied on the NLS for migration to DF-1 cell nucleus. The function of EnApiAP2 need further study.

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Section: Introductionmentioning

confidence: 99%

Localization in vivo and in vitro confirms EnApiAP2 protein encoded by ENH_00027130 as a nuclear protein in Eimeria necatrix

Cai,

Feng,

Wang

et al. 2023

Front. Cell. Infect. Microbiol.

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Advancements in understanding chicken coccidiosis: from Eimeria biology to innovative control strategies

Gao,

Sun,

et al. 2024

One Health Adv.

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Coccidiosis, an intestinal disease caused by Eimeria protozoan parasites, affects various animal species, and especially poses a significant threat to the poultry industry. The current primary control methods include anticoccidial drugs and vaccines. However, emerging challenges such as drug resistance and vaccine efficacy issues are rooted in the complex life cycle and species diversification of Eimeria. In this review, we first consolidate recent breakthroughs in understanding Eimeria biology, focusing on the parasite development and its intricate interactions with the host, notably its relationships with host immune cells and the gut microbiota. Furthermore, we provide an extensive summary of current control strategies for Eimeria infections. This includes an in-depth analysis of anticoccidial drugs, their mechanisms of resistance, and the increasing utilization of diverse anticoccidial vaccines to combat these challenges. Finally, we highlight the latest innovative strategies leading the way in coccidiosis control. Through an exploration of cutting-edge techniques, we also provide insights into future directions for effectively combating this disease. In conclusion, the future of coccidiosis control lies in the use of a multifaceted approach, integrating advanced biological insights with innovative therapeutic strategies. This review not only serves to enhance our understanding of Eimeria biology but also provides a valuable resource for researchers involved in developing and implementing strategies to manage and control coccidiosis, ensuring the health and productivity of poultry worldwide.

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iTRAQ-based proteomic analysis reveals invasion-related proteins among three developmental stages of Eimeria necatrix

Cited by 2 publications

References 54 publications

Localization in vivo and in vitro confirms EnApiAP2 protein encoded by ENH_00027130 as a nuclear protein in Eimeria necatrix

Localization in vivo and in vitro confirms EnApiAP2 protein encoded by ENH_00027130 as a nuclear protein in Eimeria necatrix

Advancements in understanding chicken coccidiosis: from Eimeria biology to innovative control strategies

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