A single S1034C mutation confers altered drug sensitivity to PfMDR1 ATPase activity that is characteristic of the 7G8 isoform

Jacqueline K. Lekostaj; Linda E. Amoah; Paul D. Roepe

doi:10.1016/j.molbiopara.2007.09.008

A single S1034C mutation confers altered drug sensitivity to PfMDR1 ATPase activity that is characteristic of the 7G8 isoform

Jacqueline K. Lekostaj, Linda E. Amoah, Paul D. Roepe

Tumor Biology Program

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

15 Citations (Scopus)

Abstract

The mechanism behind how PfMDR1 may contribute to antimalarial drug resistance is unclear. Transfection studies suggest that PfMDR1 mutations may make small contributions to drug sensitivity in a strain-dependent fashion, whereas field data link over expression (not necessarily mutation) of the gene with clinical drug treatment failure. This study dissects the contribution of individual mutations of PfMDR1 that contribute to the unique behavior of the 7G8 PfMDR1 isoform. A single mutation in putative TM 11 (S1034C) is found to abolish drug stimulation of PfMDR1 ATPase activity.

Original language	English
Pages (from-to)	107-111
Number of pages	5
Journal	Molecular and Biochemical Parasitology
Volume	157
Issue number	1
DOIs	https://doi.org/10.1016/j.molbiopara.2007.09.008
Publication status	Published - Jan 2008
Externally published	Yes

Keywords

ATPase
Drug
Malaria
PfMDR1
Vacuole

UN SDGs

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

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10.1016/j.molbiopara.2007.09.008

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abstract = "The mechanism behind how PfMDR1 may contribute to antimalarial drug resistance is unclear. Transfection studies suggest that PfMDR1 mutations may make small contributions to drug sensitivity in a strain-dependent fashion, whereas field data link over expression (not necessarily mutation) of the gene with clinical drug treatment failure. This study dissects the contribution of individual mutations of PfMDR1 that contribute to the unique behavior of the 7G8 PfMDR1 isoform. A single mutation in putative TM 11 (S1034C) is found to abolish drug stimulation of PfMDR1 ATPase activity.",

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AU - Lekostaj, Jacqueline K.

AU - Amoah, Linda E.

AU - Roepe, Paul D.

PY - 2008/1

Y1 - 2008/1

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AB - The mechanism behind how PfMDR1 may contribute to antimalarial drug resistance is unclear. Transfection studies suggest that PfMDR1 mutations may make small contributions to drug sensitivity in a strain-dependent fashion, whereas field data link over expression (not necessarily mutation) of the gene with clinical drug treatment failure. This study dissects the contribution of individual mutations of PfMDR1 that contribute to the unique behavior of the 7G8 PfMDR1 isoform. A single mutation in putative TM 11 (S1034C) is found to abolish drug stimulation of PfMDR1 ATPase activity.

KW - ATPase

KW - Drug

KW - Malaria

KW - PfMDR1

KW - Vacuole

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AN - SCOPUS:36448955049

SN - 0166-6851

VL - 157

SP - 107

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JO - Molecular and Biochemical Parasitology

JF - Molecular and Biochemical Parasitology

IS - 1

ER -

A single S1034C mutation confers altered drug sensitivity to PfMDR1 ATPase activity that is characteristic of the 7G8 isoform

Abstract

Keywords

UN SDGs

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