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Disruption of Plasmodium falciparum histidine-rich protein 2 may affect haem metabolism in the blood stage

December 15, 2020 - 16:03 -- Open Access
Author(s): 
Yang Y, Tang T, Feng B, Li S, Hou N, Ma X, Jiang L, Xin X, Chen Q
Reference: 
Parasit Vectors. 2020 Dec 9;13(1):611

Haem is a key metabolic factor in the life cycle of the malaria parasite. In the blood stage, the parasite acquires host haemoglobin to generate amino acids for protein synthesis and the by-product haem for metabolic use. The malaria parasite can also synthesize haem de novo on its own. Plasmodium falciparum-specific histidine-rich protein 2 (PfHRP2) has a haem-binding site to mediate the formation of haemozoin, a biocrystallized form of haem aggregates. Notably, the gene regulates the mechanism of haemoglobin-derived haem metabolism and the de novo haem biosynthetic pathway in the Pfhrp2-disrupted parasite line during the intraerythrocytic stages.

PV1 Protein from Plasmodium falciparum Exhibits Chaperone-Like Functions and Cooperates with Hsp100s

November 19, 2020 - 13:10 -- Open Access
Author(s): 
Hakamada K, Nakamura M, Yohda M, et al.
Reference: 
Int J Mol Sci. 2020 Nov 16;21(22):E8616

Plasmodium falciparum parasitophorous vacuolar protein 1 (PfPV1), a protein unique to malaria parasites, is localized in the parasitophorous vacuolar (PV) and is essential for parasite growth. Previous studies suggested that PfPV1 cooperates with the Plasmodium translocon of exported proteins (PTEX) complex to export various proteins from the PV.

Optimization of a Plasmodium falciparum circumsporozoite protein repeat vaccine using the tobacco mosaic virus platform

February 17, 2020 - 15:01 -- Open Access
Author(s): 
Langowski MD, Khan FA, Dutta S, et al.
Reference: 
Proc Natl Acad Sci U S A. 2020 Feb 11;117(6):3114-3122

Plasmodium falciparum vaccine RTS,S/AS01 is based on the major NPNA repeat and the C-terminal region of the circumsporozoite protein (CSP). RTS,S-induced NPNA-specific antibody titer and avidity have been associated with high-level protection in naïve subjects, but efficacy and longevity in target populations is relatively low. In an effort to improve upon RTS,S, a minimal repeat-only, epitope-focused, protective, malaria vaccine was designed. Repeat antigen copy number and flexibility was optimized using the tobacco mosaic virus (TMV) display platform.

Genetic polymorphisms in malaria vaccine candidate Plasmodium falciparum reticulocyte-binding protein homologue-5 among populations in Lagos, Nigeria

January 7, 2020 - 15:09 -- Open Access
Author(s): 
Olusola Ajibaye, Akinniyi A. Osuntoki, Alfred Amambua-Ngwa, et al.
Reference: 
Malaria Journal 2020 19:6, 6 January 2020

Vaccines are the most reliable alternative to elicit sterile immunity against malaria but their development has been hindered by polymorphisms and strain-specificity in previously studied antigens. New vaccine candidates are therefore urgently needed. Highly conserved Plasmodium falciparum reticulocyte-binding protein homologue-5 (PfRH5) has been identified as a potential candidate for anti-disease vaccine development. PfRH5 is essential for erythrocyte invasion by merozoites and crucial for parasite survival. However, there is paucity of data on the extent of genetic variations on PfRH5 in field isolates of Plasmodium falciparum. This study described genetic polymorphisms at the high affinity binding polypeptides (HABPs) 36718, 36727, 36728 of PfRH5 in Nigerian isolates of P. falciparum. This study tested the hypothesis that only specific conserved B and T cell epitopes on PfRH5 HABPs are crucial for vaccine development.

Not Open Access | Anopheles gambiae Circumsporozoite Protein–Binding Protein Facilitates Plasmodium Infection of Mosquito Salivary Glands

September 6, 2013 - 18:50 -- NOT Open Access
Author(s): 
Jiuling Wang, Yue Zhang, Yang O. Zhao, Michelle W. M. Li, Lili Zhang, Srdjan Dragovic, Nabil M. Abraham and Erol Fikrig
Reference: 
J Infect Dis. (2013) 208 (7): 1161-1169
MalariaWorld

We identified an Anopheles salivary gland protein, named CSP-binding protein (CSPBP), that interacts with CSP. Downregulation of CSPBP in mosquito salivary glands inhibited invasion by Plasmodium organisms

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