Interaction of Plasmodium falciparum apicortin with α- and β-tubulin is critical for parasite growth and survival

Sci Rep. 2021 Feb 25;11(1):4688. doi: 10.1038/s41598-021-83513-5.


Cytoskeletal structures of Apicomplexan parasites are important for parasite replication, motility, invasion to the host cell and survival. Apicortin, an Apicomplexan specific protein appears to be a crucial factor in maintaining stability of the parasite cytoskeletal assemblies. However, the function of apicortin, in terms of interaction with microtubules still remains elusive. Herein, we have attempted to elucidate the function of Plasmodium falciparum apicortin by monitoring its interaction with two main components of parasite microtubular structure, α-tubulin-I and β-tubulin through in silico and in vitro studies. Further, a p25 domain binding generic drug Tamoxifen (TMX), was used to disrupt PfApicortin-tubulin interactions which led to the inhibition in growth and progression of blood stage life cycle of P. falciparum.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing / metabolism*
  • Microtubules / metabolism
  • Plasmodium falciparum / growth & development
  • Plasmodium falciparum / metabolism*
  • Protein Binding
  • Protozoan Proteins / metabolism*
  • Tubulin / metabolism*


  • Adaptor Proteins, Signal Transducing
  • Protozoan Proteins
  • Tubulin
  • apicortin protein, Plasmodium falciparum