Endocytosis-mediated vacuolar accumulation of the human ApoE apolipoprotein-derived ApoEdpL-W antimicrobial peptide contributes to its antifungal activity in Candida albicans.

ABSTRACT: The 18-amino-acid cationic, tryptophan-rich ApoEdpL-W peptide derived from human ApoE apolipoprotein was shown to have antifungal activity against pathogenic yeasts of the Candida genus (except C. glabrata). ApoEdpL-W was active against planktonic cells and early-stage biofilms but less active against mature biofilms, possibly because of its affinity for extracellular matrix beta-glucans. Moreover, ApoEdpL-W absorbed to medically relevant materials partially prevented the formation of biofilms on these materials. The exposure of C. albicans cells to sublethal doses of ApoEdpL-W triggered a transcriptional response reminiscent of that associated with the inactivation of the MYO5 gene required for endocytosis as well as the upregulation of amino acid transporter genes. A fluorescent derivati

SUBMITTER: Rossignol T 

PROVIDER: S-EPMC3186967 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature