Date of Award

2021

Degree Type

Thesis

Degree Name

Master of Science (MS)

Department

Biological Science

Abstract

Microtubules facilitate major cellular and morphological changes in eukaryotic cells, including the protozoan parasite Plasmodium. Microtubule-associated proteins (MAPs), only very few of which have been characterized in the malaria parasite, regulate the highly dynamic microtubules. Thioredoxin-like associated protein 2 (TLAP2) is a MAP unique to the phylum apicomplexa, which in addition to Plasmodium includes the important human pathogen Toxoplasma. Here we report on the cloning and microtubule-binding activity of TLAP2 of the rodent malaria parasite Plasmodium berghei (PbTLAP2). PbTLAP2 is coded by a single exon gene and consists of 598 amino acids. The protein contains a putative C-terminal microtubule-binding domain. We investigated potential microtubule-binding capabilities of PbTLAP2 by expressing recombinant PbTLAP2-Myc in the human U2-OS cell line. Immunofluorescence imaging shows specific decoration of microtubules with PbTLAP2-myc. We furthermore demonstrate that the C-terminal 253 amino acids are sufficient for association with microtubules. Considering this, we investigated the ability of PbTLAP2 to stabilize microtubules in U2-OS cells either during cold treatment or during treatment with the microtubule-destabilizing agent nocodazole. We observed that depolymerization of microtubules was significantly reduced in the presence of PbTLAP2-Myc during cold treatment, but not during nocodazole treatment. Our data show that PbTLAP2 can act as a microtubule-binding and -stabilizing protein and may, therefore, play a significant role in the regulation of microtubules in the malaria parasite. Further studies will give new insights into the cell biology of the malaria parasite and may open new avenues for malaria intervention.

Creative Commons License

Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.

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