Histidine-rich domain of the knob protein of the human malaria parasite Plasmodium falciparum.

Kilejian, Araxie; Sharma, Yagya D.; Karoui, Hakim; Näslund, Lars-Åke

doi:10.1073/pnas.83.20.7938

Cited by 28 publications

(17 citation statements)

References 31 publications

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“…KAHRP is then transported to the red cell membrane where it induces knobs by interacting with several host as well as parasite derived molecules [4]. Earlier, we have reported the cloning and sequencing of the KAHRP gene from a Gambian isolate FCR3 [3,5]. Here, we report the sequence of KAHRP gene from two Indian isolates of P falciparum, indicating that they are different.…”

Section: Introductionmentioning

confidence: 81%

“…Both of these cytoadherent phenomena are shown to be knob mediated [14,16]. The knobless parasites, which were produced during long term cultures in the lab, were found to have lost their virulence and the capacity to synthesize KAHRP [2,3,[17][18][19]. The molecular reagents to cease the knob formation will therefore be useful to treat the falciparum malaria.…”

Section: Discussionmentioning

confidence: 99%

“…This protein is synthesized by ring and early trophozoite stages of the parasite [3]. KAHRP is then transported to the red cell membrane where it induces knobs by interacting with several host as well as parasite derived molecules [4].…”

Section: Introductionmentioning

confidence: 99%

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Allelic forms of the knob associated histidine‐rich protein gene of Plasmodium falciparum

Kant

Sharma

1996

FEBS Letters

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The knob associated histidine-rich protein (KAHRP) gene was cloned and sequenced from two Indian isolates of Plasmodiumfalciparum, Pf3-92 and Pf29-92. These isolates showed major sequence differences in the C-terminal repeat domain of KAHRP. However, the biologically important domains such as spectrin-actin binding region remained highly conserved. The PCR amplification of a variable C-terminal repeat domain from the clinical isolates of P. falciparum, from Rajasthan epidemic, showed the presence of multiple alleles of KAHRP gene. The presence of multiple alleles indicates the existence of several P. falciparum strains in India. This should be taken into account for future malaria control strategies such as molecular therapy and vaccines.

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Section: Introductionmentioning

confidence: 81%

Section: Discussionmentioning

confidence: 99%

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Allelic forms of the knob associated histidine‐rich protein gene of Plasmodium falciparum

Kant

Sharma

1996

FEBS Letters

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“…These structures are essential for the survival of the parasite in the host, and their induction requires the synthesis of the knob protein by the parasite [8][9][10][11][12][13][14] . These knobs are rich in histidine.…”

Section: Discussionmentioning

confidence: 99%

A comparative laboratory diagnosis of malaria: microscopy versus rapid diagnostic test kits

Azikiwe

Ifezulike

Siminialayi

et al. 2012

Asian Pacific Journal of Tropical Biomedicine

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“…However, a number of proteins that are directed past the PVM to the erythrocyte cytosol do not have classical N-terminal signals. Instead, proteins such as the knob-associated histidine-rich protein (KAHRP) have a hydrophobic stretch of amino acids starting 20 -80 amino acids from the N terminus (13,17). This "internal" hydrophobic signal does not appear to function in heterologous trafficking systems, since KAHRP is not translocated across the ER membrane in a cell-free system using mammalian microsomes (9,16,18).…”

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confidence: 99%

The Signal Sequence of Exported Protein-1 Directs the Green Fluorescent Protein to the Parasitophorous Vacuole of Transfected Malaria Parasites

Adisa¹,

Rug²,

Klonis

et al. 2003

Journal of Biological Chemistry

114

108

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The malaria parasite, Plasmodium falciparum, spends part of its life cycle inside the erythrocytes of its human host. In the mature stages of intraerythrocytic growth, the parasite undertakes extensive remodeling of its adopted cellular home by exporting proteins beyond the confines of its own plasma membrane. To examine the signals involved in export of parasite proteins, we have prepared transfected parasites expressing a chimeric protein comprising the N-terminal region of the Plasmodium falciparum exported protein-1 appended to green fluorescent protein. The majority of the population of the chimeric protein appears to be correctly processed and trafficked to the parasitophorous vacuole, indicating that this is the default destination for protein secretion. Some of the protein is redirected to the parasite food vacuole and further degraded. Photobleaching studies reveal that the parasitophorous vacuole contains subcompartments that are only partially interconnected. Dual labeling with the lipid probe, BODIPY-TR-ceramide, reveals the presence of membrane-bound extensions that can bleb from the parasitophorous vacuole to produce double membranebound compartments. We also observed regions and extensions of the parasitophorous vacuole, where there is segregation of the lumenal chimera from the lipid components. These regions may represent sites for the sorting of proteins destined for the trafficking to sites beyond the parasitophorous vacuole membrane.Due to the compartmentalization of eukaryotic cells, a sophisticated protein trafficking system is an integral requirement for homeostasis and growth. Proteins destined for compartments other than the cytoplasm are synthesized with intrinsic signals that determine their transport within the cell. Small peptide motifs often form the necessary targeting determinants (1). For example, an N-terminal hydrophobic sequence forms part of the typical secretory signal that directs proteins across the endoplasmic reticulum (ER) 1 membrane (2-5). Similarly, N-terminal amphipathic and bipartite sequences target proteins to the chloroplast and mitochondria (6 -8).The malaria parasite, Plasmodium falciparum, spends part of its life cycle inside mature human erythrocytes. The parasite invades this quiescent host cell and develops within a parasitophorous vacuole (PV). An unusual and highly specialized secretory system enables the malaria parasite to survive within a cell that lacks its own machinery for protein synthesis and trafficking. Indeed, the parasite targets proteins, not only to compartments within its own confines, but to the PV, in which it resides, as well as the PV membrane (PVM), the erythrocyte cytoplasm, and host cell membrane (9 -11).Efforts have been made to understand the trafficking signals that target parasite proteins to different compartments within and outside the parasite. Proteins destined for the ER, the parasite plasma membrane (PPM), the PV, or the PVM appear to have a "classical" hydrophobic N-terminal signal sequence (i.e. a stretch of 10 -15 hydrop...

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Histidine-rich domain of the knob protein of the human malaria parasite Plasmodium falciparum.

Cited by 28 publications

References 31 publications

Allelic forms of the knob associated histidine‐rich protein gene of Plasmodium falciparum

Allelic forms of the knob associated histidine‐rich protein gene of Plasmodium falciparum

A comparative laboratory diagnosis of malaria: microscopy versus rapid diagnostic test kits

The Signal Sequence of Exported Protein-1 Directs the Green Fluorescent Protein to the Parasitophorous Vacuole of Transfected Malaria Parasites

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