Arbuscular mycorrhizal fungi confer enhanced arsenate resistance on Holcus lanatus

The role of arbuscular mycorrhizal fungi (AMF) in arsenate resistance in arbuscular mycorrhizal associations is investigated here for two Glomus spp. isolated from the arsenate-resistant grass Holcus lanatus. Glomus mosseae and Glomus caledonium were isolated from H. lanatus growing on an arsenic-contaminated mine-spoil soil. The arsenate resistance of spores was compared with nonmine isolates using a germination assay. Short-term arsenate influx into roots and long-term plant accumulation of arsenic by plants were also investigated in uninfected arsenate resistant and nonresistant plants and in plants infected with mine and nonmine AMF. Mine AMF isolates were arsenate resistant compared with nonmine isolates. Resistant and nonresistant G. mosseae both suppressed high-affinity arsenate/phosphate transport into the roots of both resistant and nonresistant H. lanatus. Resistant AMF colonization of resistant H. lanatus growing in contaminated mine spoil reduced arsenate uptake by the host. We conclude that AMF have evolved arsenate resistance, and conferred enhanced resistance on H. lanatus.

Phylloseptin-PBa—A Novel Broad-Spectrum Antimicrobial Peptide from the Skin Secretion of the Peruvian Purple-Sided Leaf Frog (Phyllomedusa Baltea) Which Exhibits Cancer Cell Cytotoxicity

Antimicrobial peptides from amphibian skin secretion display remarkable broad-spectrum antimicrobial activity and are thus promising for the discovery of new antibiotics. In this study, we report a novel peptide belonging to the phylloseptin family of antimicrobial peptides, from the skin secretion of the purple-sided leaf frog, Phyllomedusa baltea, which was named Phylloseptin-PBa. Degenerate primers complementary to putative signal peptide sites of frog skin peptide precursor-encoding cDNAs were designed to interrogate a skin secretion-derived cDNA library from this frog. Subsequently, the peptide was isolated and identified using reverse phase HPLC and MS/MS fragmentation. The synthetic replicate was demonstrated to have activity against S. aureus, E. coli and C. albicans at concentrations of 8, 128 and 8 mg/L, respectively. In addition, it exhibited anti-proliferative activity against the human cancer cell lines, H460, PC3 and U251MG, but was less active against a normal human cell line (HMEC). Furthermore, a haemolysis assay was performed to assess mammalian cell cytotoxicity of Phylloseptin-PBa. This peptide contained a large proportion of α-helical domain, which may explain its antimicrobial and anticancer activities.