<i>Plasmodium falciparum</i>protein ‘PfJ23’ hosts distinct binding sites for major virulence factor ‘PfEMP1’ and Maurer's cleft marker ‘PfSBP1’

Kaur, Jasweer; Kumar, Vikash; Singh, Amrit Pal; Singh, Vineeta; Bisht, Anjali; Dube, Taru; Panda, Jiban Jyoti; Behl, Ankita; Mishra, Prakash Chandra; Hora, Rachna

doi:10.1093/femspd/fty090

Cited by 4 publications

(4 citation statements)

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“…[60] PfEMP1 needs to successfully interact with a plethora of proteins in order to reach the RBC surface. [101] PfEMP1, RIFIN, STEVOR, and PfMC-2TM belong to the group of Plasmodium protein families that are also known as variant surface antigens (VSA) due to their role in the rosetting of infected RBC and immune evasion. [96,102] Although the MC are very prominent structures within the infected RBC, there are several proteins within the cytoplasm that are neither resident nor transiently connected with the organelle.…”

Section: The Structure and Morphology Of The Maurer's Clefts Througho...mentioning

confidence: 99%

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Novel secretory organelles of parasite origin ‐ at the center of host‐parasite interaction

Bekić,

Kilian

2023

BioEssays

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Reorganization of cell organelle‐deprived host red blood cells by the apicomplexan malaria parasite Plasmodium falciparum enables their cytoadherence to endothelial cells that line the microvasculature. This increases the time red blood cells infected with mature developmental stages remain within selected organs such as the brain to avoid the spleen passage, which can lead to severe complications and cumulate in patient death. The Maurer's clefts are a novel secretory organelle of parasite origin established by the parasite in the cytoplasm of the host red blood cell in order to facilitate the establishment of cytoadherence by conducting the trafficking of immunovariant adhesins to the host cell surface. Another important function of the organelle is the sorting of other proteins the parasite traffics into its host cell. Although the organelle is of high importance for the pathology of malaria, additional putative functions, structure, and genesis remain shrouded in mystery more than a century after its discovery. In this review, we highlight our current knowledge about the Maurer's clefts and other novel secretory organelles established within the host cell cytoplasm by human‐pathogenic malaria parasites and other parasites that reside within human red blood cells.

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Section: The Structure and Morphology Of The Maurer's Clefts Througho...mentioning

confidence: 99%

“…[ 60 ] PfEMP1 needs to successfully interact with a plethora of proteins in order to reach the RBC surface. [ 101 ]…”

Section: Discovery Structure and Function Of The Maurer's Cleftsmentioning

confidence: 99%

Novel secretory organelles of parasite origin ‐ at the center of host‐parasite interaction

Bekić,

Kilian

2023

BioEssays

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“…These proteins were purified according to protocols described in Kumar et al [28] and Kaur et al [49].…”

Section: 6mentioning

confidence: 99%

“…Different proteins (1µg each) i.e. rcCBP2 (positive control), BR5 domain of PfSBP1 [48], and negative controls (ATS domain of PfEMP1 [49] and BSA) were immobilized on NC membrane and blocked with 5% BSA in 1X PBS for 2 hrs at room temperature (RT). After blocking, blots were washed with 1X PBS and probed with rcCBP2 (20 µg/ 5ml) for 1hr at RT.…”

Section: Dot-blot Assaymentioning

confidence: 99%

CX3CL1 binding protein-2 (CBP2) of Plasmodium falciparum binds nucleic acids

Saxena

Kaur

Hora

et al. 2019

International Journal of Biological Macromolecules

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Several exported Plasmodium falciparum(Pf) proteins contribute to malaria biology through their involvement in cytoadherence, immune evasion and host cell remodelling. Many of these exported proteins and other host molecules are present in iRBC (infected red blood cell) generated extracellular vesicles (EVs), which are responsible for host cell modification and parasite development. CX3CL1 binding proteins (CBPs) present on the surface of iRBC have been reported to contribute to cytoadhesion by binding with the chemokine 'CX3CL1' via their extracellular domains. Here, we have characterized the cytoplasmic domain of CBP2to understand its function in parasite biology using biochemical and biophysical methods.Recombinant cytoplasmic CBP2 (rcCBP2) binds nucleic acids showing interaction with DNA/RNA. rcCBP2 shows dimer formation under non-reducing conditions highlighting the role of disulphide bonds in oligomerization while ATP binding leads to structural changes in the protein. In vitro interaction studies depict its binding with a Maurer's cleft resident protein 'PfSBP1', which is influenced by ATP binding of rcCBP2. Our results suggest CBP2 as a two-

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PfEMP1 and var genes – Still of key importance in Plasmodium falciparum malaria pathogenesis and immunity

Hviid,

Jensen,

Deitsch

2024

Advances in Parasitology

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Plasmodium falciparumprotein ‘PfJ23’ hosts distinct binding sites for major virulence factor ‘PfEMP1’ and Maurer's cleft marker ‘PfSBP1’

Cited by 4 publications

References 52 publications

Novel secretory organelles of parasite origin ‐ at the center of host‐parasite interaction

Novel secretory organelles of parasite origin ‐ at the center of host‐parasite interaction

CX3CL1 binding protein-2 (CBP2) of Plasmodium falciparum binds nucleic acids

PfEMP1 and var genes – Still of key importance in Plasmodium falciparum malaria pathogenesis and immunity

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