Ascalin, a new anti-fungal peptide with human immunodeficiency virus type 1 reverse transcriptase-inhibiting activity from shallot bulbs.
An isolation procedure comprising ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography on SP-Sepharose and gel filtration on Superdex 75 was used to isolate an anti-fungal peptide from the bulbs of the shallot Allium ascalonicum. The peptide demonstrated a molecular weight of 9.5kDa, and possessed an N-terminal sequence YQCGQGG somewhat similar to chitinases from other Allium species which are however much larger in molecular weight. The peptide designated ascalin manifested a unique specific anti-fungal activity. It inhibited mycelial growth in the fungus Botrytis cinerea but not in the fungi Mycosphaerella arachidicola and Fusarium oxysporum. Ascalin inhibited HIV-1 reverse transcriptase with an IC(50) of 10 microM, much more potently than Allium tuberosum anti-fungal protein and other anti-fungal proteins.
Wang
H X
HX
Department of Microbiology, College of Biological Science, China Agricultural University, Beijing, China.
Ng
T B
TB
D000935:Antifungal Agents / Q000494:pharmacology*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D054303:HIV Reverse Transcriptase / Q000037:antagonists & inhibitors*; D020128:Inhibitory Concentration 50; D037102:Lectins / Q000378:metabolism; D010455:Peptides / Q000737:chemistry*; D028321:Plant Preparations / Q000494:pharmacology; D010940:Plant Proteins / Q000737:chemistry* / Q000494:pharmacology*; D017434:Protein Structure, Tertiary; D018894:Reverse Transcriptase Inhibitors / Q000494:pharmacology*; D027781:Shallots / Q000378:metabolism
D000935:Antifungal Agents; D037102:Lectins; D010455:Peptides; D028321:Plant Preparations; D010940:Plant Proteins; D018894:Reverse Transcriptase Inhibitors; C471567:ascalin protein, shallot; D054303:HIV Reverse Transcriptase