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Department of Clinical Laboratory Sciences

Soluble expression of plasmodium falciparum glutamine synthetase and three-dimensional structure by single particle reconstruction

Abstract

dc:description.abstract

[No subject] Malaria infection caused by the apicomplexa pathogen Plasmodium falciparum has a high rate of resistance to existing anti-malarial drugs. The World Health Organisation recommended interventions are unlikely to eliminate the growth of resistance and it would therefore be prudent to continue the search for new drug targets for the continued combatting of malaria. Plasmodium falciparum is parasitic on the host for its metabolites and therefore inhibiting the transportation of glutamine from the host, has long been considered a potential strategy for combating the spread of infection. The recently sequenced Plasmodium falciparum genome has however shown that pathways for independent survival are also conserved. Therefore, combating the spread of Plasmodium falciparum in the human host, in addition to inhibiting the transportation of glutamine, will also require the inhibition of the de novo expression of essential amino acids within the Plasmodium falciparum cell. This could be achieved by inhibiting the glutamine synthetase gene, which is an essential step in the tri-carboxylic acid cycle.

Degree

thesis:*
Grantor dc:publisher.institution
Department of Clinical Laboratory Sciences
Year dc:date.issued
2015

Author and committee

dc:creator, dc:contributor.*
Author dc:creator
  • Patel, Satishkumar Ishverlal
Advisor dc:contributor.advisor
  • Sewell, Trevor

Rights

Language dc:language.iso
eng

Identifiers

dc:identifier.*
Handle dc:identifier.uri
http://hdl.handle.net/11427/17429
OAI identifier oai:identifier
oai:open.uct.ac.za:11427/17429

Chain of custody

source
Harvested from
University of Cape Town
Base URL
open.uct.ac.za/oai/request
Last updated
2026-07-22
Source record
OAI-PMH GetRecord
related terms
citation

Patel, Satishkumar Ishverlal. Soluble expression of plasmodium falciparum glutamine synthetase and three-dimensional structure by single particle reconstruction. Department of Clinical Laboratory Sciences, 2015. http://hdl.handle.net/11427/17429