Antibiotic inhibitors of organellar protein synthesis in Plasmodium falciparum

Barbara Clough; Kaveri Rangachari; Malcolm Strath; Peter R. Preiser; R. J.M. Wilson

doi:10.1016/S1434-4610(99)70021-0

Antibiotic inhibitors of organellar protein synthesis in Plasmodium falciparum

Barbara Clough^*
, Kaveri Rangachari
, Malcolm Strath
, Peter R. Preiser
, R. J.M. Wilson

^*Corresponding author for this work

Biosciences

Research output: Contribution to journal › Article › peer-review

67 Citations (Scopus)

Abstract

Elongation factor Tu (EF-Tu) is encoded by the tuf gene of the plastid organelle of the malaria parasite Plasmodium falciparum. A range of structurally unrelated inhibitors of this GTP-dependent translation factor was shown to have antimalarial activity in blood cultures. The most active was the cyclic thiazolyl peptide amythiamicin A with an IC⁵⁰ = 0.01 μM. Demonstrable complexes were formed in vitro between a recombinant version of P. falciparum EF-Tu(pl) and inhibitors that bind to different sites on EF-Tu; these included the antibiotics kirromycin, GE2270A and enacyloxin IIa.

Original language	English
Pages (from-to)	189-195
Number of pages	7
Journal	Protist
Volume	150
Issue number	2
DOIs	https://doi.org/10.1016/S1434-4610(99)70021-0
Publication status	Published - Aug 1999

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

ASJC Scopus subject areas

Microbiology

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10.1016/S1434-4610(99)70021-0

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title = "Antibiotic inhibitors of organellar protein synthesis in Plasmodium falciparum",

abstract = "Elongation factor Tu (EF-Tu) is encoded by the tuf gene of the plastid organelle of the malaria parasite Plasmodium falciparum. A range of structurally unrelated inhibitors of this GTP-dependent translation factor was shown to have antimalarial activity in blood cultures. The most active was the cyclic thiazolyl peptide amythiamicin A with an IC50 = 0.01 μM. Demonstrable complexes were formed in vitro between a recombinant version of P. falciparum EF-Tu(pl) and inhibitors that bind to different sites on EF-Tu; these included the antibiotics kirromycin, GE2270A and enacyloxin IIa.",

author = "Barbara Clough and Kaveri Rangachari and Malcolm Strath and Preiser, \{Peter R.\} and Wilson, \{R. J.M.\}",

year = "1999",

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T1 - Antibiotic inhibitors of organellar protein synthesis in Plasmodium falciparum

AU - Clough, Barbara

AU - Rangachari, Kaveri

AU - Strath, Malcolm

AU - Preiser, Peter R.

AU - Wilson, R. J.M.

PY - 1999/8

Y1 - 1999/8

N2 - Elongation factor Tu (EF-Tu) is encoded by the tuf gene of the plastid organelle of the malaria parasite Plasmodium falciparum. A range of structurally unrelated inhibitors of this GTP-dependent translation factor was shown to have antimalarial activity in blood cultures. The most active was the cyclic thiazolyl peptide amythiamicin A with an IC50 = 0.01 μM. Demonstrable complexes were formed in vitro between a recombinant version of P. falciparum EF-Tu(pl) and inhibitors that bind to different sites on EF-Tu; these included the antibiotics kirromycin, GE2270A and enacyloxin IIa.

AB - Elongation factor Tu (EF-Tu) is encoded by the tuf gene of the plastid organelle of the malaria parasite Plasmodium falciparum. A range of structurally unrelated inhibitors of this GTP-dependent translation factor was shown to have antimalarial activity in blood cultures. The most active was the cyclic thiazolyl peptide amythiamicin A with an IC50 = 0.01 μM. Demonstrable complexes were formed in vitro between a recombinant version of P. falciparum EF-Tu(pl) and inhibitors that bind to different sites on EF-Tu; these included the antibiotics kirromycin, GE2270A and enacyloxin IIa.

UR - https://www.scopus.com/pages/publications/0033180232

U2 - 10.1016/S1434-4610(99)70021-0

DO - 10.1016/S1434-4610(99)70021-0

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AN - SCOPUS:0033180232

SN - 1434-4610

VL - 150

SP - 189

EP - 195

JO - Protist

JF - Protist

IS - 2

ER -

Antibiotic inhibitors of organellar protein synthesis in Plasmodium falciparum

Abstract

UN SDGs

ASJC Scopus subject areas

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