Journals / Erciyes Üniversitesi Veteriner Fakültesi Dergisi / 2017 / Cilt: 14 - Sayı: 1

Apicoplast in Apicomplexan Protozoon

Apicomplexan Protozoonlarda Apicoplast

Pages
49–59
Publication Date
2022-10-18
DOI
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AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

In this review, it was aimed to point out the apicoplast and to s hare the data about some functions of this organel.

📌 3 Key Takeaways

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Objective & Hypothesis:Protistan species belonging to the subphylum apicomplexa have a non-photosynthetic secondary plastid structure also called apicoplast.
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Key Findings & Data:This organel is found in most parasitic genera of apicomplexan protozoans like Plasmodium, Eimeria, Toxoplasma, Sarcocystis, Theileria and Babesia spp., but not in the ohers such as Cryptosporidium spp. and Gregarina niphandrodes.
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Conclusion & Impact:In this review, it was aimed to point out the apicoplast and to s hare the data about some functions of this organel.
🔬Design:Review & Systematic Survey
📍Scope:Comprehensive Sample
⚙️Variables:Apicomplexan · apicoplast · evrim

Abstract

Protistan species belonging to the subphylum apicomplexa have a non-photosynthetic secondary plastid structure also called apicoplast. This organel is found in most parasitic genera of apicomplexan protozoans like Plasmodium, Eimeria, Toxoplasma, Sarcocystis, Theileria and Babesia spp., but not in the ohers such as Cryptosporidium spp. and Gregarina niphandrodes. It is believed that the apicoplast is originated from an alga (red or green alga) through secondary endosymbiosis. The apicoplast is surrounded by fourfold membrane within the outer most part of the endomembrane system. The apicoplast which is a highly specialized organelle that mediates required functions in the growth and replication of apicomplexan parasites contains an ensemble of bacteria-like pathways to replicate and express its genome plus an anabolic capacity generating fatty acids, heme and isoprenoid precursors. Destroying this organel usually results in parasite death, thus making apicoplast metabolism an attractive target for drugs. However, the data about the functions of the apicoplast are limited and there are some hyppotehesis about this subject. In this review, it was aimed to point out the apicoplast and to s hare the data about some functions of this organel.

Özet

Apicomplexa subphylumunda bulunan protistan türleri fotosentetik olmayan apicoplast adı verilen ikincil bir plastide sahiptirler. Apicoplast; Plasmodium, Eimeria, Toxoplasma, Sarcocystis, Theileria ve Babesia gibi bazı apicomplexan protozoonlarda bulunan buna karşılık Cryptosporidium spp ve Gregarina niphandrodes’de bulunmayan bir plastiddir. Apicoplastın sekonder endosimbiyoz ile bir algden (kırmızı ya da yeşil alg) evrimleştiğine inanılmaktadır. Apicoplast, endomembran sisteminin en dış bölümü içinde dört membran tarafından çevrelenmiştir. Apicomplexan parazitlerinin büyümesi ve replikasyonu için gerekli son derece özelleşmiş bir organel olan apicoplastın bakterilerde varolan yağ asidi sentezi, hem pathwayi ve isoprenoid biyosentezine sahip olduğu bilinmektedir. Bu organelin yıkımlanması bu parazitlerde ölüme yol açmaktadır. Bu durum, ilaç endüstrisinin protozoonlara karşı ilaç geliştirme çalışmalarında odak noktasını oluşturmuştur. Bu yüzden ilaç endüstrisi araştırmalarını bu organele ait gen bölgeleri üzerine yoğunlaştırmıştır. Bununla birlikte apicoplastın işlevleri hakkındaki bilgiler henüz yeterli olmayıp bu konuda çeşitli hipotezler mevcuttur. Bu derlemede apicoplasta dikkat çekilmesi ve bazı fonksiyonları hakkında üretilen bilgilerin paylaşılması amaçlanmıştır.

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Cite This Article

YILDIRIM, A., İNCİ, A., ŞAHİNGÖZ, G. D., DÜZLÜ, Ö. (2022). Apicoplast in Apicomplexan Protozoon. Erciyes Üniversitesi Veteriner Fakültesi Dergisi, Cilt: 14 - Sayı: 1, 49–59. https://ajindex.com/articles/503824

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References (10)

  1. Abrahamsen MS, Templeton TJ, Enomoto S, Abrahante JE, Zhu G, Lancto CA, DengM, Liu C,Widmer G, Tzipori S, Buck GA, Xu P, Bankier AT, Dear PH, Konfortov BA, Spriggs HF, Iyer L, Anantharaman V, Aravind L, Kapur V. Complete genome sequence of the apicomplexan, Cryptosporidium parvum. Science 2004
  2. 304(5669): 441-5. 2. Adl SM, Leander BS, Simpson AG, Archibald JM, Anderson OR, Bass D, Bowser SS, Brugerolle G, Farmer MA, Karpov S, Kolisko M, Lane CE, Lodge DJ, Mann DG, Meisterfeld R, Mendoza L, Moestrup O, Mozley-Standridge SE, Smirnov AV, Spiegel F. Diversity, nomenclature, and taxonomy of protists. Syst Biol 2007
  3. 56(4): 684-9. 3. Adl SM, Simpson AG, Farmer MA, Andersen RA, Anderson OR, Barta JR, Bowser SS, Brugerolle G, Fensome RA, Fredericq S, James TY, Karpov S, Kugrens P, Krug J, Lane CE, Lewis LA, Lodge J, Lynn DH, Mann DG, McCourt RM, Mendoza L, Moestrup O, Mozley-Standridge SE, Nerad TA, Shearer CA, Smirnov AV, Spiegel FW, Taylor MF.The new higher level classification of eukaryotes with emphasis on the taxonomy of protists. J Eukaryot Microbiol 2005
  4. 52(5): 399-451. 4. Apt KE, Clendennen SK, Powers DA, Grossman AR. The gene family encoding the fucoxanthin chlorophyll proteins from the brown alga Macrocystis pyrifera. Mol Gen Genet 1995
  5. 246(4): 455-64. 5. Blatter E, Ross W, Tang H, Gourse R, Ebright R. Domain organization of RNA polymerase a subunit: C-terminal 85 amino acids constitute a domain capable of dimerization and DNA binding. Cell 1994
  6. 78(5): 889-96. 6. Bolte K, Bullmann L, Hempel F, Bozarth A, Zauner S, Maier UG. Protein targeting into secondary plastids. J Eukaryot Microbiol 2009
  7. 56(1): 9-15. 7. Brayton KA, Lau AO, Herndon DR, Hannick L, Kappmeyer LS, Berens SJ, Bidwell SL, Brown WC, Crabtree J, Fadrosh D, Feldblum T, Forberger HA, Haas BJ, Howell JM, Khouri H, Koo H, Mann DJ, Norimine J, Paulsen IT, Radune D, Ren Q, Smith RK Jr, Suarez CE, White O, Wortman JR, Knowles DP Jr, McElwain TF, Nene VM. Genome sequence of Babesia bovis and comparative analysis of apicomplexan hemoprotozoa. PLoS Pathog 2007
  8. 3(10): 1401-13. 8. Cai X, Fuller AL, McDougald LR, Zhu G. Apicoplast genome of the coccidian Eimeria tenella Gene 2003
  9. 4(321): 39-46. 9. Clastre M, Goubard A, Prel A, Mincheva Z, Viaud-Massuart MC, Bout D, Rideau M, Velge-Roussel F, Laurent F. The methylerythritol phosphate pathway for isoprenoid biosynthesis in coccidia: presence and sensitivity to fosmidomycin. Exp Parasitol 2007
  10. 116(4): 375-84. 10. Denny P, Preiser P, Williamson D, Wil