Tubulin in the Erythrocytic Stages of Plasmodium falciparum

Martin Read

    Research output: ThesisMaster's Thesis

    Abstract

    A procedure for the preparation of Plasmodium falciparum parasites for immunofluorescence was developed, which enabled the internal fine structure of these cells to be preserved. This allowed the clear visualisation of microtubular structures and their changing conformation through the erythrocytic cell-cycle, to the stage of cytodifferentiation leading to merozoite release. The images of spindle development observed, together with an analysis of the number of nuclear bodies occurring per cell in a large number of parasites, indicated an apparent asynchrony in the process of chromosomal multiplication. The use of antibodies specific for post-translational modification of alpha-tubulin, demonstrated that the C-terminal tyrosine-containing epitope of P. falciparum alpha-tubulin I is similar to that of other organisms. Lysine-40 in the same molecule, a target for highly specific in vivo acetylation in some organisms, was found to be unmodified in blood stage parasites. After in vitro acetylation of this residue, however, the epitope to which lysine-40 contributes was recognized by antibody, showing that the conformation of this part of the molecule is also conserved, despite a lack of primary sequence homology immediately downstream of the target lysine residue.
    Original languageEnglish
    QualificationMaster of Science
    Awarding Institution
    • UMIST
    Supervisors/Advisors
    • Hyde, John, Supervisor
    Place of PublicationJRLUM
    Publisher
    Publication statusPublished - 1995

    Keywords

    • Tubulin, microtubules, mitosis, mitotic spindle, asynchrony, malaria, Plasmodium falciparum

    Research Beacons, Institutes and Platforms

    • Manchester Institute of Biotechnology

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