
TY  - JOUR
A1  - Harrison, Stuart J. 
A1  - Marcus, John P. 
A1  - Goulter, Kenneth C. 
A1  - Green, Jodie L. 
A1  - Maclean, Donald J. 
A1  - Manners, John M. 
T1  - An Antimicrobial Peptide from the Australian Native <emph type="2">Hardenbergia violacea</emph> Provides the First Functionally Characterised Member of a Subfamily of Plant Defensins
JF  - Functional Plant Biology
JO  - Functional Plant Biol.
Y1  - 1997
VL  - 24
IS  - 5
SP  - 571
EP  - 578
KW  - Plant defence, cowpea, pea, thionins, &#945;-amylase inhibitors, protein synthesis inhibitor, antifungal activity, Fabaceae.
UR  - https://doi.org/10.1071/PP97075 
N2  - An antimicrobial peptide (HvAMP1) was isolated from seeds of the Australian native legume Hardenbergia violacea (Schneev.) Stearn. The peptide is 47 amino acid residues in length, contains 8 cysteines, and has a molecular weight of 5392 and a predicted pI of 10.41. HvAMP1 inhibited the growth of several plant pathogenic fungi at concentrations as low as 1 &#181;M in vitro and produced distinct hyphal distortion and increased branching. This antimicrobial activity was greatly diminished in the presence of 1 mM CaCl2 and 50 mM KCl. The purified peptide at 40 &#181;M did not inhibit three different a-amylase enzymes. Aeukaryotic cell-free translation system showed inhibition approaching 50% in the presence of ~100 &#181;M of HvAMP1. The viability of plant and mammalian cells cultured in vitro was not adversely affected by concentrations of HvAMP1 as high as 40 mM. The amino acid sequence of HvAMP1 contained the consensus amino acids that define the plant defensin family of peptides. The HvAMP1 amino acid sequence showed 87% and 57% identity with the amino acid sequences deduced from cDNA sequences from defensins of Vigna unguiculata and Pisum sativum, respectively. Other plant defensin sequences showed less than 33% amino acid identity to the peptide. Therefore, HvAMP1 and the putative plant defensins of cowpea and pea define a distinct sequence subfamily of plant defensins which is at present limited to members of the Fabaceae. HvAMP1 is the first member of this subfamily to be purified and functionally characterised. The antimicrobial activity of HvAMP1 suggests a defensive role for this subfamily of peptides. 
ER  -

