Molecular basis for resistance of acanthamoeba tubulins to all major classes of antitubulin compounds

Fiona L. Henriquez; Paul R. Ingram; Stephen P. Muench; David W. Rice; Craig W. Roberts

doi:10.1128/AAC.00355-07

Molecular basis for resistance of acanthamoeba tubulins to all major classes of antitubulin compounds

Fiona L. Henriquez
, Paul R. Ingram
, Stephen P. Muench
, David W. Rice
, Craig W. Roberts

Strathclyde Institute Of Pharmacy And Biomedical Sciences

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

33 Citations (Scopus)

82 Downloads (Pure)

Abstract

Tubulin is essential to eukaryotic cells and is targeted by several antineoplastics, herbicides, and antimicrobials. We demonstrate that Acanthamoeba spp. are resistant to five antimicrotubule compounds, unlike any other eukaryote studied so far. Resistance correlates with critical amino acid differences within the inhibitor binding sites of the tubulin heterodimers.

Original language	English
Pages (from-to)	1133-1135
Number of pages	3
Journal	Antimicrobial Agents and Chemotherapy
Volume	52
Issue number	3
DOIs	https://doi.org/10.1128/AAC.00355-07
Publication status	Published - Mar 2008

UN SDGs

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

SDG 3 Good Health and Well-being

Keywords

molecular chemistry
acanthamoeba tubulins
anti-tubulin compounds
pharmacology

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10.1128/AAC.00355-07

Antimicrob. Agents Chemother.-2008-Henriquez-1133-5Final published version, 268 KB

Cite this

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abstract = "Tubulin is essential to eukaryotic cells and is targeted by several antineoplastics, herbicides, and antimicrobials. We demonstrate that Acanthamoeba spp. are resistant to five antimicrotubule compounds, unlike any other eukaryote studied so far. Resistance correlates with critical amino acid differences within the inhibitor binding sites of the tubulin heterodimers.",

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language = "English",

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AU - Henriquez, Fiona L.

AU - Ingram, Paul R.

AU - Muench, Stephen P.

AU - Rice, David W.

AU - Roberts, Craig W.

PY - 2008/3

Y1 - 2008/3

N2 - Tubulin is essential to eukaryotic cells and is targeted by several antineoplastics, herbicides, and antimicrobials. We demonstrate that Acanthamoeba spp. are resistant to five antimicrotubule compounds, unlike any other eukaryote studied so far. Resistance correlates with critical amino acid differences within the inhibitor binding sites of the tubulin heterodimers.

AB - Tubulin is essential to eukaryotic cells and is targeted by several antineoplastics, herbicides, and antimicrobials. We demonstrate that Acanthamoeba spp. are resistant to five antimicrotubule compounds, unlike any other eukaryote studied so far. Resistance correlates with critical amino acid differences within the inhibitor binding sites of the tubulin heterodimers.

KW - molecular chemistry

KW - acanthamoeba tubulins

KW - anti-tubulin compounds

KW - pharmacology

U2 - 10.1128/AAC.00355-07

DO - 10.1128/AAC.00355-07

M3 - Article

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SN - 0066-4804

VL - 52

SP - 1133

EP - 1135

JO - Antimicrobial Agents and Chemotherapy

JF - Antimicrobial Agents and Chemotherapy

IS - 3

ER -

Molecular basis for resistance of acanthamoeba tubulins to all major classes of antitubulin compounds

Abstract

UN SDGs

Keywords

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