title: An antifungal protein from Bacillus amyloliquefaciens.
abstract: OBJECTIVE
  To isolate and characterize an antifungal protein from the culture broth of the bacterium Bacillus amyloliquefaciens.
  
  
  RESULTS
  The antifungal protein designated as baciamin was isolated and exhibited a molecular mass around 50 kDa. Baciamin manifested a broad spectrum of antifungal activity. Baciamin could induce membrane permeabilization of tested fungi. Its antifungal activity was retained after incubation with trypsin and EDTA. Various ions tested did not affect its antifungal activity. Baciamin reduced the activity of HIV-1 reverse transcriptase (RT). It also inhibited proliferation of hepatoma, breast cancer and colon cancer cell lines. Baciamin augmented nitric oxide production by mouse macrophages.
  
  
  CONCLUSIONS
  Bacillus amyloliquefaciens produces a broad-spectrum antifungal protein, baciamin. It induces membrane permeabilization in fungi but not in rabbit erythrocytes. Its antifungal activity is relatively thermostable, pH- and trypsin-stable. It demonstrates antiproliferative activity towards various tumour cells, nitric oxide-inducing activity towards macrophages, and inhibitory activity towards HIV-1 RT.
  
  
  CONCLUSIONS
  Baciamin represents one of the few bacterial antifungal proteins reported to date. Most of the previously isolated antifungal molecules of bacterial origin are either peptides or ring compounds. Baciamin also exhibits other exploitable activities such as antitumour and immuno-enhancing activities.
authors.affiliation: Department of Biochemistry, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, NT, Hong Kong, China.
authors.forename: J H
authors.initials: JH
authors.lastname: Wong
authors.forename: J
authors.initials: J
authors.lastname: Hao
authors.forename: Z
authors.initials: Z
authors.lastname: Cao
authors.forename: M
authors.initials: M
authors.lastname: Qiao
authors.forename: H
authors.initials: H
authors.lastname: Xu
authors.forename: Y
authors.initials: Y
authors.lastname: Bai
authors.forename: T B
authors.initials: TB
authors.lastname: Ng
mesh_terms: D000818:Animals; D000935:Antifungal Agents / Q000302:isolation & purification / Q000494:pharmacology*; D000970:Antineoplastic Agents / Q000302:isolation & purification / Q000494:pharmacology*; D001407:Bacillus / Q000737:chemistry*; D001419:Bacteria / Q000187:drug effects*; D045744:Cell Line, Tumor / Q000378:metabolism; D049109:Cell Proliferation / Q000187:drug effects; D004492:Edetic Acid; D054303:HIV Reverse Transcriptase / Q000037:antagonists & inhibitors / Q000378:metabolism; D051379:Mice; D008826:Microbial Sensitivity Tests; D009569:Nitric Oxide / Q000378:metabolism; D010455:Peptides / Q000302:isolation & purification / Q000494:pharmacology*; D010940:Plant Proteins / Q000302:isolation & purification / Q000494:pharmacology*; D014357:Trypsin
chemical_list: D000935:Antifungal Agents; D000970:Antineoplastic Agents; D010455:Peptides; D010940:Plant Proteins; D009569:Nitric Oxide; D004492:Edetic Acid; C514824:reverse transcriptase, Human immunodeficiency virus 1; D054303:HIV Reverse Transcriptase; D014357:Trypsin