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dc.contributor.authorNonlawat Boonyalaien_US
dc.contributor.authorPichamon Sittikulen_US
dc.contributor.authorJirundon Yuvaniyamaen_US
dc.contributor.otherKasetsart Universityen_US
dc.contributor.otherMahidol Universityen_US
dc.date.accessioned2018-11-23T09:42:43Z-
dc.date.available2018-11-23T09:42:43Z-
dc.date.issued2015-05-29en_US
dc.identifier.citationMolecular and Biochemical Parasitology. Vol.201, No.1 (2015), 5-15en_US
dc.identifier.issn18729428en_US
dc.identifier.issn01666851en_US
dc.identifier.other2-s2.0-84930667506en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84930667506&origin=inwarden_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/35453-
dc.description.abstract© 2015 Elsevier B.V. All rights reserved. Plasmepsin V from Plasmodium falciparum (PfPMV) is responsible for the cleavage of the Plasmodium export element (PEXEL) motif at the N-terminus of several hundreds of the exported proteins. PfPMV is necessary for parasite viability and has become a novel promising target for antimalarial therapy. The first recombinant expression of soluble, active PfPMV as thioredoxin fusion proteins is reported herein. Two truncated forms of PfPMV were fused to thioredoxin (Trx) to generate Trx-PfPMVp37 and Trx-PfPMVm84. The fusion proteins were successfully purified using Ni<sup>2+</sup> affinity chromatography in combination with ATP treatment to eliminate Escherichia coli HSP60 contaminant. Trx-PfPMVm84 could hydrolyze the PEXEL-containing peptides more efficiently than Trx-PfPMVp37. Interestingly, both Trx-PfPMVs preferred to cleave PfEMP2 peptide over HRPII peptide. The replacement of Ser with Val or Glu at P<inf>1</inf>′ position created a substrate with 75% reduction in the enzyme activity, whereas the substitution of Ile with Lys or Glu at P<inf>2</inf> position reduced the cleavage efficiency by 30%. The activity of Trx-PfPMVm84 was inhibited by PMSF and nelfinavir but not by pepstatin A. After the removal of Trx domain, activities of both enzymes toward PfEMP2 and HRPII peptides were fitted to the Michaelis-Menten model to determine kinetic parameters. The K<inf>m</inf> values toward both peptides were apparently much lower than the previously reported data although with similar k<inf>cat</inf> values. Along with an improved PfPMV preparation protocol, these findings have provided insights into its substrate specificity at P<inf>2</inf> and P<inf>1</inf>′ positions as well as interactions among the enzyme, substrates, and inhibitors.en_US
dc.rightsMahidol Universityen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84930667506&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.subjectImmunology and Microbiologyen_US
dc.titlePlasmodium falciparum Plasmepsin v (PfPMV): Insights into recombinant expression, substrate specificity and active site structureen_US
dc.typeArticleen_US
dc.rights.holderSCOPUSen_US
dc.identifier.doi10.1016/j.molbiopara.2015.05.004en_US
Appears in Collections:Scopus 2011-2015

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