DmAMP1, an antifungal plant defensin from dahlia (<i>Dahlia merckii</i>), interacts with sphingolipids from<i>Saccharomyces cerevisiae</i>

Thevissen, Karin; François, Isabelle; Takemoto, Jon Y.; Ferket, Kathelijne K.A.; Meert, Els; Cammue, Bruno P. A.

doi:10.1016/s0378-1097(03)00590-1

Cited by 101 publications

(86 citation statements)

References 29 publications

(37 reference statements)

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“…It has been shown that sphingolipids and sterols are enriched in specific domains in the plasma membranes, the so-called membrane rafts (31,32). We demonstrated recently that the interaction between the dahlia plant defensin DmAMP1 and inositolphosphoryl-containing sphingolipids from S. cerevisiae is enhanced by 40% in the presence of equimolar concentrations of ergosterol (12), pointing toward a putative involvement of rafts in the DmAMP1 interaction with the fungal plasma membrane. This is in contrast to the interaction between RsAFP2 and fungal GlcCer, which is not altered by different concentrations of ergosterol.…”

Section: Discussionmentioning

confidence: 84%

“…In a similar approach, we demonstrated recently the positive effect of ergosterol on the interaction of DmAMP1 with sphingolipids from S. cerevisiae (12). Interaction of 50 nM RsAFP2 with different concentrations of ergosterol (ranging from 0.1 nmol to 5 nmol coated/well) was assessed.…”

Section: Rsafp2 Interacts With Fungal Glccer But Not With Soybean or mentioning

confidence: 97%

“…Possibly, membrane patches containing sphingolipids act as binding sites for DmAMP1. Interaction between DmAMP1 and these sphingolipids could lead to insertion of the plant defensin into the membrane resulting in membrane destabilization (10,12).…”

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confidence: 99%

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Defensins from Insects and Plants Interact with Fungal Glucosylceramides

Thevissen¹,

Warnecke

François³

et al. 2004

Journal of Biological Chemistry

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326

310

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Growth of the yeast species Candida albicans andPichia pastoris is inhibited by RsAFP2, a plant defensin isolated from radish seed (Raphanus sativus), at micromolar concentrations. In contrast, gcs-deletion mutants of both yeast species are resistant toward RsAFP2. GCS genes encode UDP-glucose:ceramide glucosyltransferases, which catalyze the final step in the biosynthesis of the membrane lipid glucosylceramide. In an enzymelinked immunosorbent assay-based binding assay, RsAFP2 was found to interact with glucosylceramides isolated from P. pastoris but not with soybean nor human glucosylceramides. Furthermore, the P. pastoris parental strain is sensitive toward RsAFP2-induced membrane permeabilization, whereas the corresponding gcs-deletion mutant is highly resistant to RsAFP2-mediated membrane permeabilization. A model for the mode of action of RsAFP2 is presented in which all of these findings are linked. Similarly to RsAFP2, heliomicin, a defensin-like peptide from the insect Heliothis virescens, is active on C. albicans and P. pastoris parental strains but displays no activity on the gcs-deletion mutants of both yeast species. Furthermore, heliomicin interacts with glucosylceramides isolated from P. pastoris and soybean but not with human glucosylceramides. These data indicate that structurally homologous antifungal peptides present in species from different eukaryotic kingdoms interact with the same target in the fungal plasma membrane, namely glucosylceramides, and as such support the hypothesis that defensins from plants and insects have evolved from a single precursor.

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Section: Discussionmentioning

confidence: 84%

Section: Rsafp2 Interacts With Fungal Glccer But Not With Soybean or mentioning

confidence: 97%

See 1 more Smart Citation

Defensins from Insects and Plants Interact with Fungal Glucosylceramides

Thevissen¹,

Warnecke

François³

et al. 2004

Journal of Biological Chemistry

Self Cite

326

310

View full text Add to dashboard Cite

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“…However, some bacteria, particularly Grampositive species, are also inhibited, although the activity is less pronounced than that against fungi. The growth of several fungal species, including several filamentous fungi and yeast cells, was inhibited when incubated with these peptides [7][8][9][10][11][12][13][14][15][16][17][18][19][20][21]. Despite the broad inhibitory activity that plant defensins exhibit against different micro-organisms, scientists know little about their activity against protozoa.…”

Section: Introductionmentioning

confidence: 99%

PvD1 defensin, a plant antimicrobial peptide with inhibitory activity against Leishmania amazonensis

et al. 2015

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SynopsisPlant defensins are small cysteine-rich peptides and exhibit antimicrobial activity against a variety of both plant and human pathogens. Despite the broad inhibitory activity that plant defensins exhibit against different micro-organisms, little is known about their activity against protozoa. In a previous study, we isolated a plant defensin named PvD 1 from Phaseolus vulgaris (cv. Pérola) seeds, which was seen to be deleterious against different yeast cells and filamentous fungi. It exerted its effects by causing an increase in the endogenous production of ROS (reactive oxygen species) and NO (nitric oxide), plasma membrane permeabilization and the inhibition of medium acidification. In the present study, we investigated whether PvD 1 could act against the protozoan Leishmania amazonensis. Our results show that, besides inhibiting the proliferation of L. amazonensis promastigotes, the PvD 1 defensin was able to cause cytoplasmic fragmentation, formation of multiple cytoplasmic vacuoles and membrane permeabilization in the cells of this organism. Furthermore, we show, for the first time, that PvD 1 defensin was located within the L. amazonensis cells, suggesting the existence of a possible intracellular target.

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“…The interaction between DmAMP and the yeast membrane could probably occur directly without the involvement of membrane proteins [9,10] and it probably leads to an insertion of the defensin into the membrane, resulting in an alteration of the membrane property and inhibition of fungal growth [11].…”

Section: Introductionmentioning

confidence: 99%

The hydrophobic surface of PaAMP from pokeweed seeds is essential to its interaction with fungal membrane lipids and the antifungal activity

et al. 2005

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PaAMP is a small seed-specific antimicrobial protein from pokeweeds. It has a cysteine-knot fold with a positive patch and a hydrophobic surface. Site-specific mutagenesis was performed to study the roles of these two domains in antimicrobial activity and we found that the mutations in the hydrophobic surface had a more profound effect than that in the positive patch. A protein-membrane interaction was observed with the green fluorescence protein-PaAMP (GFP-AMP) fusion protein. The mutations that replace the amino acid residues forming hydrophobic surface with neutral residues abolished the interaction of PaAMP with the membrane and the binding of PaAMP to fungal sphingolipids while ergosterol enhanced the binding, suggesting that the hydrophobic surface was required for the interaction between PaAMP and fungal plasma membrane lipid raft.

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DmAMP1, an antifungal plant defensin from dahlia (Dahlia merckii), interacts with sphingolipids fromSaccharomyces cerevisiae

Cited by 101 publications

References 29 publications

Defensins from Insects and Plants Interact with Fungal Glucosylceramides

Defensins from Insects and Plants Interact with Fungal Glucosylceramides

PvD1 defensin, a plant antimicrobial peptide with inhibitory activity against Leishmania amazonensis

The hydrophobic surface of PaAMP from pokeweed seeds is essential to its interaction with fungal membrane lipids and the antifungal activity

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