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Expression and characterization of functional domains of FK506-binding protein 35 from Plasmodium knowlesi

Carlmond Kah Wun Goh1, Jovi Silvester1, Wan Nur Shuhaida Wan Mahadi1

  • 1Biotechnology Research Institute, Universiti Malaysia Sabah, Kota Kinabalu, Sabah, Malaysia.

Protein Engineering, Design & Selection : PEDS
|May 24, 2019
PubMed

Insights

Plasmodium knowlesi FK506-binding protein (Pk-FKBP35) shows antimalarial potential. Its FK506-binding domain (FKBD) is crucial for catalytic activity and calcineurin inhibition, while the tetratricopeptide repeat domain (TPRD) facilitates dimerization.

Area of Science:

  • Malariology
  • Structural Biology
  • Drug Discovery

Background:

  • Plasmodium knowlesi FK506-binding protein (Pk-FKBP35) is a peptidyl-prolyl cis-trans isomerase (PPIase) and a potential antimalarial target.
  • Pk-FKBP35 comprises an N-terminal FK506-binding domain (FKBD) and a C-terminal tetratricopeptide repeat domain (TPRD).

Purpose of the Study:

  • To elucidate the functional roles of Pk-FKBP35 domains for novel antimalarial drug development.
  • To characterize the catalytic and structural properties of Pk-FKBP35 and its isolated domains.

Main Methods:

  • Overexpression, purification, and characterization of full-length Pk-FKBP35, Pk-FKBD, and Pk-TPRD.
  • Site-directed mutagenesis to identify key catalytic residues within Pk-FKBD.
  • Assays for PPIase activity, oligomerization, and inhibition of calcineurin phosphatase activity.

Main Results:

  • Catalytic PPIase activity resides in the full-length Pk-FKBP35 and Pk-FKBD, indicating FKBD-mediated catalysis.
  • Pk-TPRD is essential for Pk-FKBP35 dimerization.
  • Specific residues (Asp55, Arg60, Trp77, Phe117) in Pk-FKBD are critical for PPIase activity; FKBD is essential for calcineurin inhibition, with TPRD potentially aiding binding.

Conclusions:

  • Pk-FKBP35's FKBD is the catalytic domain and essential for calcineurin inhibition, a key target for antimalarial strategies.
  • The TPRD domain plays a role in protein dimerization, potentially influencing interactions with cellular targets.
  • Understanding Pk-FKBP35 domain functions provides a basis for designing targeted antimalarial drugs.
Keywords:
Plasmodium knowlesiFk506-binding protein (FKBP)Malariafunctional domainpeptidyl-prolyl cis-trans isomerase (PPIase)

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