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

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

28 Citations (Scopus)

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
Externally published	Yes

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title = "Molecular basis for resistance of Acanthamoeba tubulins to all major classes of antitubulin compounds",

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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AU - Henriquez, Fiona. L

AU - Ingram, Paul R.

AU - Muench, Stephen P.

AU - Rice, David W.

AU - Roberts, Craig W.

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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.

U2 - 10.1128/AAC.00355-07

DO - 10.1128/AAC.00355-07

M3 - Article

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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

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