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

Ritu Saxena1, Jasweer Kaur2, Rachna Hora2

  • 1Department of Biotechnology, Guru Nanak Dev University, Amritsar, Punjab 143005, India.

International Journal of Biological Macromolecules
|July 30, 2019
PubMed

Insights

Plasmodium falciparum CBP2 protein

Area of Science:

  • Malariology
  • Cell Biology
  • Molecular Parasitology

Background:

  • Plasmodium falciparum (Pf) exported proteins are crucial for malaria pathogenesis, influencing cytoadherence, immune evasion, and host cell remodeling.
  • Infected red blood cell (iRBC)-derived extracellular vesicles (EVs) carry proteins and host molecules, mediating host cell modification and parasite development.
  • CX3CL1 binding proteins (CBPs) on iRBC surfaces facilitate cytoadhesion by interacting with the chemokine CX3CL1 via their extracellular domains.

Purpose of the Study:

  • To characterize the cytoplasmic domain of CBP2 (cCBP2) and elucidate its function in Plasmodium falciparum biology.
  • To investigate the biochemical and biophysical properties of cCBP2, including its interactions with nucleic acids and other proteins.
  • To understand the role of cCBP2 in targeting EVs and delivering cargo to host endothelial cells.

Main Methods:

  • Biochemical and biophysical techniques were employed to characterize recombinant cCBP2.
  • Nucleic acid binding assays were performed to assess interactions with DNA and RNA.
  • Protein-protein interaction studies, including in vitro binding assays with PfSBP1, were conducted.
  • The influence of ATP binding on cCBP2 structure and interactions was investigated.

Main Results:

  • Recombinant cCBP2 demonstrated binding affinity for both DNA and RNA.
  • cCBP2 exhibited dimer formation under non-reducing conditions, indicating the importance of disulfide bonds for oligomerization.
  • ATP binding induced structural alterations in cCBP2.
  • In vitro studies revealed that cCBP2 binds to PfSBP1, a Maurer's cleft resident protein, with ATP binding modulating this interaction.

Conclusions:

  • CBP2 functions as a two-transmembrane (2TM) receptor involved in targeting EVs and delivering cargo to host endothelial cells.
  • The cytoplasmic domain of CBP2 plays a role in nucleic acid binding and interacts with PfSBP1, potentially influencing parasite biology.
  • CBP2 is proposed as a key molecule mediating cytoadherence through its extracellular domain and immune modulation via its cytoplasmic domain.
Keywords:
ATPExtracellular vesicles (EVs)Infected RBCsNucleic acid binding proteinPfSBP1RNA/DNA

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