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Open Access research with a European policy impact...

The Strathprints institutional repository is a digital archive of University of Strathclyde's Open Access research outputs. Strathprints provides access to thousands of Open Access research papers by Strathclyde researchers, including by researchers from the European Policies Research Centre (EPRC).

EPRC is a leading institute in Europe for comparative research on public policy, with a particular focus on regional development policies. Spanning 30 European countries, EPRC research programmes have a strong emphasis on applied research and knowledge exchange, including the provision of policy advice to EU institutions and national and sub-national government authorities throughout Europe.

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Acanthamoeba alternative oxidase genes : identification, characterisation and potential as antimicrobial targets

Henriquez, Fiona L. and McBride, James and Campbell, Sara J. and Ramos, Tania and Ingram, Paul R. and Roberts, F. and Tinney, Sinead and Roberts, C.W. (2009) Acanthamoeba alternative oxidase genes : identification, characterisation and potential as antimicrobial targets. International Journal for Parasitology, 39 (13). pp. 1417-1424. ISSN 0020-7519

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Abstract

Alternative oxidase (AOX) is a mitochondrial protein that acts as an alternative terminal oxidase to the conventional cytochrome oxidases. It is present in certain prokaryotes, plants, fungi and some protozoa but absent in mammals. AOX activity has previously been described in Acanthamoeba, although no genetic evidence has been reported. Herein, two AOX (AcAOX) genes designated isoforms A and B, were obtained from Acanthamoeba castellanii by a combination of degenerate PCR from cDNA and a series of 5′ and 3′ rapid amplification of cDNA ends. The corresponding genomic sequences of these AcAOXs were also obtained. Each gene spans six exons over a region of 1607 and 1619 bp, respectively. Isoforms A and B have open reading frames of 1113 and 1125 bp, respectively. Each encodes a protein with a predicted molecular weight of 42 kDa. Each AcAOX protein has a predicted cleavable mitochondrial targeting sequence. The full-length AcAOX is functionally active as it complements hemL-deficient Escherichia coli and inhibited by the inhibitor of AOX, salicylhydroxamic acid (SHAM). SHAM is effective against A. castellanii and Acanthamoeba polyphaga only when used in conjunction with antimycin A, an inhibitor of the conventional cytochrome respiratory pathway. Transcripts for AcAOX are increased during the encystment process, indicating a possible role for alternative respiration during stress.