Kugler M, Loeffler W, Rapp C, Kern A, Jung G
Institut für Mikrobiologie I, Universität Tübingen, Federal Republic of Germany.
Arch Microbiol. 1990;153(3):276-81. doi: 10.1007/BF00249082.
Rhizocticin A, the main component of the antifungal, hydrophilic phosphono-oligopeptides of Bacillus subtilis ATCC 6633, was used for sensitivity testing and experiments into the molecular mechanism of the antibiotic action. Budding and filamentous fungi as well as the cultivated nematode Caenorhabditis elegans were found to be sensitive, whereas bacteria and the protozoon Paramecium caudatum were insensitive. Rhizoctonia solani was inhibited in agar dilution tests but not in diffusion tests. The antifungal effect of rhizocticin A was neutralized by a variety of amino acids and oligopeptides. Oligopeptide influence was mainly understood as transport antagonism, and it was concluded that the antibiotic enters the recipient cell via the peptide transport system. L- and D-cystine were also identified as potent, general antagonists of the oligopeptide transport. The rhizocticin-antagonism of four other amino acids was taken as a clue to the site of action. Provided that rhizocticin A is split by peptidases of the target cell into inactive L-arginine and toxic L-2-amino-5-phosphono-3-cis-pentenoic acid (L-APPA), the latter may interfere with the threonine or threonine-related metabolism.
枯草芽孢杆菌ATCC 6633产生的抗真菌亲水性膦酰基寡肽的主要成分根际菌素A，被用于敏感性测试和抗生素作用分子机制的实验。发现出芽和丝状真菌以及培养的线虫秀丽隐杆线虫对其敏感，而细菌和尾草履虫原生动物则不敏感。在琼脂稀释试验中茄丝核菌受到抑制，但在扩散试验中未受抑制。根际菌素A的抗真菌作用被多种氨基酸和寡肽中和。寡肽的影响主要被理解为转运拮抗作用，并且得出结论，该抗生素通过肽转运系统进入受体细胞。L-和D-胱氨酸也被鉴定为寡肽转运的有效通用拮抗剂。另外四种氨基酸对根际菌素的拮抗作用被视为作用位点的线索。如果根际菌素A被靶细胞的肽酶分解成无活性的L-精氨酸和有毒的L-2-氨基-5-膦酰基-3-顺式-戊烯酸（L-APPA），后者可能会干扰苏氨酸或与苏氨酸相关的代谢。
