scholarly journals Potensi Kombinasi Ekstrak Daun Kelor (Moringa oliefera) dan Artemisia (Artemisia annua) Sebagai Antimalaria Plasmodium falciparum

2020 ◽  
Vol 12 (2) ◽  
pp. 831-841
Author(s):  
Elvina Veronica ◽  
Irene Amelia ◽  
Kezia Angelina Yunatan ◽  
Ni Kadek Sinta Dwi Chrismayanti ◽  
Agung Nova Mahendra
Keyword(s):  
Plasmodium Falciparum ◽  
Combination Therapy ◽  
Protease Inhibitor ◽  
Cysteine Protease ◽  
Plasmodium Berghei ◽  
Artemisia Annua ◽  
Cysteine Protease Inhibitor

Penatalaksanaan malaria seperti kloroquine dan Artemisin Combination Therapy dapat memberikan efek samping dan sudah mengalami resistensi sehingga diperlukan alternatif pengobatan lain. Metode penulisan ini menggunakan kajian pustaka dari sejumlah literatur valid dan relevan. Artemisinin pada tanaman Artemisia annua menghambat PfATPase6 sehingga membuat homeostasis Ca plasmodium terganggu dan menghambat pertumbuhan plasmodium. Enzim cysteine protease, inhibitor ALLN, Plasmepsin-2 serta Plasmepsin-1 berfungsi menghancurkan plasmodium pada fase trophozoite dan schizont dengan mendegradasi protein plasmodium. Flavonoid pada daun kelor (Moringa oliefera) meningkatkan produksi Hb dan mengoptimalkan kinerja artemisin. Kaempferol dan antioksidan lainnya pada daun kelor menghambat pertumbuhan plasmodium lewat jalur permeasi baru dengan menghambat pembentukan membrane saat fase intraeritrositik dan menghambat proses degradasi hemoglobin sehingga plasmodium tidak dapat berkembang. Kandungan daun kelor juga dapat memenuhi kebutuhan gizi per hari dan mengatasi malnutrisi. Kombinasi artemisia dan daun kelor berpotensi sebagai alternatif obat malaria akibat infeksi plasmodium falciparum karena kombinasi kedua zat tersebut terbukti lebih efektif menghambat plasmodium berghei pada hewan uji coba, meningkatkan sistem imun, serta memenuhi kebutuhan gizi dibandingkan penggunaan artemisin maupun daun kelor secara tunggal. Perlu penelitian lebih lanjut terkait hal tersebut.

scholarly journals A Cysteine Protease Inhibitor of Plasmodium berghei Is Essential for Exo-erythrocytic Development

2014 ◽  
Vol 10 (8) ◽  
pp. e1004336 ◽  
Author(s):  
Christine Lehmann ◽  
Anna Heitmann ◽  
Satish Mishra ◽  
Paul-Christian Burda ◽  
Mirko Singer ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Cysteine Protease ◽  
Plasmodium Berghei ◽  
Cysteine Protease Inhibitor

scholarly journals Inhibition of Plasmodium falciparum Oocyst Production by Membrane-Permeant Cysteine Protease Inhibitor E64d

2006 ◽  
Vol 51 (3) ◽  
pp. 1064-1070 ◽  
Author(s):  
S. Eksi ◽  
B. Czesny ◽  
G.-J. van Gemert ◽  
R. W. Sauerwein ◽  
W. Eling ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Blood Cell ◽  
Protease Inhibitor ◽  
Red Blood Cell ◽  
Cysteine Protease ◽  
Malaria Parasite ◽  
Cysteine Proteases ◽  
Food Vacuole ◽  
Cysteine Protease Inhibitor ◽  
Parasite Transmission

ABSTRACT During asexual intraerythrocytic growth, Plasmodium falciparum utilizes hemoglobin obtained from the host red blood cell (RBC) as a nutrient source. Papain-like cysteine proteases, falcipains 2 and 3, have been reported to be involved in hemoglobin digestion and are targets of current antimalarial drug development efforts. However, their expression during gametocytogenesis, which is required for malaria parasite transmission, has not been studied. Many of the available antimalarials do not inhibit development of sexual stage parasites, and therefore, the persistence of gametocytes after drug treatment allows continued transmission of the disease. In the work reported here, incubation of stage V gametocytes with membrane-permeant cysteine protease inhibitor E64d significantly inhibited oocyst production (80 to 100%). The same conditions inhibited processing of gametocyte-surface antigen Pfs230 during gametogenesis but did not alter the morphology of the food vacuole in gametocytes, inhibit emergence, or block male exflagellation. E64d reduced the level of oocyst production more effectively than that reported previously for falcipain 1-knockout parasites, suggesting that falcipains 2 and 3 may also be involved in malaria parasite transmission. However, in this study only falcipain 3 and not falcipain 2 was found to be expressed in stage V gametocytes. Interestingly, during gametocytogenesis falcipain 3 was transported into the red blood cell and by stage V was localized in vesicles along the RBC surface, consistent with a role during gamete emergence. The ability of a membrane-permeant cysteine protease inhibitor to significantly reduce malaria parasite transmission suggests that future drug design should include evaluation of gametogenesis and sporogonic development.

scholarly journals Falstatin, a Cysteine Protease Inhibitor of Plasmodium falciparum, Facilitates Erythrocyte Invasion

2006 ◽  
Vol 2 (11) ◽  
pp. e117 ◽  
Author(s):  
Kailash C. Pandey ◽  
Naresh Singh ◽  
Shirin Arastu-Kapur ◽  
Matthew Bogyo ◽  
Philip J. Rosenthal
Keyword(s):  
Plasmodium Falciparum ◽  
Protease Inhibitor ◽  
Cysteine Protease ◽  
Cysteine Protease Inhibitor ◽  
Erythrocyte Invasion

scholarly journals A Novel Cysteine Protease Inhibitor of Naegleria fowleri That Is Specifically Expressed during Encystation and at Mature Cysts

Pathogens ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 388
Author(s):  
Hương Giang Lê ◽  
A-Jeong Ham ◽  
Jung-Mi Kang ◽  
Tuấn Cường Võ ◽  
Haung Naw ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Cysteine Protease ◽  
Expression Profiles ◽  
Critical Role ◽  
Cyst Formation ◽  
Cysteine Proteases ◽  
Cysteine Protease Inhibitor ◽  
Naegleria Fowleri ◽  
Nægleria Fowleri ◽  
Cystatin Family

Naegleria fowleri is a free-living amoeba that is ubiquitous in diverse natural environments. It causes a fatal brain infection in humans known as primary amoebic meningoencephalitis. Despite the medical importance of the parasitic disease, there is a great lack of knowledge about the biology and pathogenicity of N. fowleri. In this study, we identified and characterized a novel cysteine protease inhibitor of N. fowleri (NfCPI). NfCPI is a typical cysteine protease inhibitor belonging to the cystatin family with a Gln-Val-Val-Ala-Gly (QVVAG) motif, a characteristic motif conserved in the cystatin family of proteins. Bacterially expressed recombinant NfCPI has a dimeric structure and exhibits inhibitory activity against several cysteine proteases including cathespin Bs of N. fowleri at a broad range of pH values. Expression profiles of nfcpi revealed that the gene was highly expressed during encystation and cyst of the amoeba. Western blot and immunofluorescence assays also support its high level of expression in cysts. These findings collectively suggest that NfCPI may play a critical role in encystation or cyst formation of N. fowleri by regulating cysteine proteases that may mediate encystation or mature cyst formation of the amoeba. More comprehensive studies to investigate the roles of NfCPI in encystation and its target proteases are necessary to elucidate the regulatory mechanism and the biological significance of NfCPI.

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