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PFF1320C: an essential but presumptive Plasmodium myosin light chain
Dissertation   Open access

PFF1320C: an essential but presumptive Plasmodium myosin light chain

Melody Robinson Wright
Doctor of Philosophy (Ph.D.), Drexel University
Mar 2017
DOI:
https://doi.org/10.17918/etd-7526
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Abstract

Microbiology
Little is known regarding the nature and function of the myosin motors of Plasmodium. Analysis of the genome reveals that there are six myosin heavy chains but only two, PfMyoA and PfMyoB, have been characterized with the role of PfMyoA, along with its cognate light chain partner MTIP, being directly involved in the process of parasite invasion. PFF1320c is annotated in the Plasmodium genome as a putative myosin light chain but to date there is no biochemical evidence to support this designation. Interestingly, this molecule is only found in the primate malaria parasites and is not found in the rodent parasites. Preliminary studies of PFF1320c have shown that the protein is essential due to our inability to delete the gene. Expression of a tagged version of the gene at an ectopic site permitted the successful knockout of PFF1320c. Studies are currently underway to identify the myosin heavy chain (MHC) partner and other potential binding partners using PFF1320c fused to promiscuous biotin ligase (BirA*) to label proteins in close proximity to the presumptive light chain, where the 1320-BirA* fusion is also subject to translational regulation by use of a small molecule aptamer. We are also working to phenotypically elucidate the role of this presumptive actin-myosin motor within the parasite using the glmS ribozyme or the aptamer system as an alternate knockdown strategy. Further characterization of this presumptive myosin light chain and identification of the MHC partner will provide an insight into the role of this unique myosin motor in the growth and development of the parasite.

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