Journal article
Agp2p, the plasma membrane transregulator of polyamine uptake, regulates the antifungal activities of the plant defensin nad1 and other cationic peptides
MR Bleackley, JL Wiltshire, F Perrine-Walker, S Vasa, RL Burns, NL Van Der Weerden, MA AnDerson
Antimicrobial Agents and Chemotherapy | AMER SOC MICROBIOLOGY | Published : 2014
DOI: 10.1128/AAC.02087-13
Abstract
Cationic antifungal peptides (AFPs) act through a variety of mechanisms but share the common feature of interacting with the fungal cell surface. NaD1, a defensin from Nicotiana alata, has potent antifungal activity against a variety of fungi of both hyphal and yeast morphologies. The mechanism of action of NaD1 occurs via three steps: binding to the fungal cell surface, permeabilization of the plasma membrane, and internalization and interaction with intracellular targets to induce fungal cell death. The targets at each of these three stages have yet to be defined. In this study, the screening of a Saccharomyces cerevisiae deletion collection led to the identification of Agp2p as a regulato..
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Awarded by discovery project from the Australian Research Council (ARC)
Funding Acknowledgements
This work was supported by a discovery project from the Australian Research Council (ARC) (grant DP120102694 to M.A.A. and N.L. V.D.W.) and a La Trobe University Early Career Research grant (to M.R.B.).