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Identification of a lysophospholipid acyltransferase in the pathogenic yeast Candida albicans
Author(s) -
Ayyash Mariam,
Algahmi Amal,
Oelkers Peter
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.585.2
Subject(s) - candida albicans , acyltransferase , systemic candidiasis , phospholipid , yeast , biology , microbiology and biotechnology , corpus albicans , biochemistry , virulence , chemistry , gene , membrane
Candida albicans is a yeast regularly found within the mouth and gastrointestinal tract of healthy individuals. However, systemic proliferation can lead to potentially life‐threatening infections. Two classes of anti‐fungals target membrane composition and integrity, supporting that the plasma membrane is a sensitive target. Limiting phospholipid remodeling may accentuate the effects of these antifungals. To test this hypothesis, we characterized a lysophospholipid acyltransferase in C. albicans and generated a homologous deletion strain for the encoding gene, 1881. Preliminary assays have found the 1881, double deletionmutation strains to show a mild resistance to a polyene antibiotic and two azoles. C. elegans is currently being used as a host to assay the virulence of 1881 deletion strains. To understand the role of 1881p in phospholipid remodeling, we expressed it in S. cerevisiae and performed in vitro lysophospholipid acyltransferase assays to determine substrate specificity. The V max /K m ratio lead to the following ranking of substrate preference: linolenoyl CoA>; oleoyl CoA>; linoleoyl CoA>; stearoyl CoA. Mass spectrometry is being used to assess differences in cellular phospholipid species after stearate pulse – chase assays in normal and deletion strains. Funded by the Office of Sponsored Research, University of Michigan – Deaborn .