Specific binding sites for an antifungal plant defensin from Dahlia (Dahlia merckii) on fungal cells are required for antifungal activity.
作者： Karin Thevissen , Rupert W. Osborn , David P. Acland , Willem F. Broekaert
DOI: 10.1094/MPMI.2000.13.1.54
关键词: Yeast 、 Biology 、 Defensin 、 Binding site 、 Plant defensin 、 Biochemistry 、 Dahlia 、 Microbiology 、 Saccharomyces cerevisiae 、 Neurospora crassa 、 Antimicrobial peptides
摘要: Dm-AMP1, an antifungal plant defensin from seeds of dahlia (Dahlia merckii), was radioactively labeled with t-butoxycarbonyl-[35S]-L-methionine N-hydroxy-succinimi-dylester. This procedure yielded a 35S-labeled peptide unaltered activity. [35S]Dm-AMP1 used to assess binding on living cells the filamentous fungus Neurospora crassa and unicellular Saccharomyces cerevisiae. Binding fungal saturable could be competed for by preincubation excess, unlabeled Dm-AMP1 as well Ah-AMP1 Ct-AMP1, two defensins that are highly homologous Dm-AMP1. In contrast, not more distantly related or structurally unrelated antimicrobial peptides. either N. S. cerevisiae apparently irreversible. addition, whole microsomal membrane fractions independently obtained mutants selected resistance exhib...
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