BIOINFORMATIC ANALYSIS OF CANDIDA GLABRATA YBT1 AS A PUTATIVE ABC TRANSPORTER
PublisherThe University of Arizona.
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AbstractThe fungal species Candida glabrata has demonstrated azole resistance in clinical isolates (1). This resistance is likely conferred by the species’ increased expression of ATP-binding cassette (ABC) transporters at the vacuolar and plasma membrane (1). Using BLAST searches and multiple sequence alignments, C. glabrata pleiotropic ABC efflux transporter of multiple drugs (CgYbt1; UniprotKB: Q6FWS5) was identified as an ABC transporter involved in either cellular detoxification or stress response (2). To experimentally determine the structure and function of this protein, constructs were designed for overexpression in Saccharomyces cerevisiae DSY5 cultures. Further studies will aim to experimentally determine the structure, function, and subcellular location of CgYbt1. This work has the potential to offer novel insights into the C. glabrata multidrug resistance network.