Abstract
Members of the Cysteine-rich secretory protein, Antigen 5 and Pathogenesis-related 1 (CAP) protein superfamily are important virulence factors in fungi but remain poorly characterized on molecular level. Here, we investigate the cellular localization and molecular function of Rbe1p and Rbt4p, two CAP family members from the human pathogen Candida albicans. We unexpectedly found that Rbe1p localizes to budding sites of yeast cells in a disulfide bond-dependent manner. Furthermore, we show that Rbe1p and Rbt4p bind free cholesterol in vitro and export cholesteryl acetate in vivo. These findings suggest a previously undescribed role for Rbe1p in cell wall-associated processes and a possible connection between the virulence attributes of fungal CAP proteins and sterol binding.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Binding Sites
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Biological Transport
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Candida albicans / physiology*
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Candidiasis / microbiology*
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Cholesterol / chemistry
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Cholesterol / metabolism
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Fungal Proteins / chemistry
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Fungal Proteins / genetics
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Fungal Proteins / metabolism*
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Humans
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Models, Molecular
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Molecular Conformation
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Protein Binding
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Protein Interaction Domains and Motifs
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Protein Transport
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Sterols / chemistry
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Sterols / metabolism
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Structure-Activity Relationship
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Virulence
Substances
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Fungal Proteins
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Sterols
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Cholesterol
Grants and funding
Funded by Landesgraduierten Förderung Universität Stuttgart and the Swiss National Science Foundation (31003A_173003, and 31003A_153416). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.