Vv-AMP1, a ripening induced peptide from Vitis vinifera shows strong antifungal activity.

Vv-AMP1, a ripening induced peptide from Vitis vinifera shows strong antifungal activity.
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DOI:
10.1186/1471-2229-8-75
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发表时间:
2008-07-08
期刊:
影响因子:
5.3
通讯作者:
Vivier MA
Vivier MA
中科院分区:
生物学2区
文献类型:
--
作者:
de Beer A;Vivier MA

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最新研究表明,小分子抗菌肽在植物的天然防御系统中发挥作用。这些肽通常通过在发芽种子周围或植物器官内不同组织层之间形成保护屏障来促进预先形成的防御。在主动防御过程中,非生物和生物刺激也可以上调编码基因。所述肽显示出广谱的抗微生物活性。它们强大的抗病原体特性确保了它们是医学和农业生物技术部门有希望的目标。从葡萄属葡萄中分离到一个浆果特异性的cDNA序列,命名为Vv-AMP 1,即葡萄属葡萄抗菌肽1。Vv-AMP 1编码一个77个氨基酸的肽,其显示与植物防御素家族的序列同源性。Vv-AMP 1以组织特异性的、发育调节的方式表达,仅在浆果成熟开始时及以后在浆果组织中表达。用生物或非生物因子处理叶和浆果组织在测试条件下并没有导致Vv-AMP 1表达增加。预测的信号肽Vv-AMP 1,融合到绿色荧光蛋白(GFP),表明信号肽允许其产物在质外体中的积累。在大肠杆菌中产生的Vv-AMP 1肽具有5.495 kDa的分子量,如通过质谱法测定的。重组Vv-AMP 1具有极高的热稳定性,对广谱植物病原真菌表现出很强的抗真菌活性,对枯萎病病原体尖孢镰刀菌和大丽轮枝菌具有非常高的活性水平。Vv-AMP 1肽没有诱导处理的真菌菌丝的形态变化,而是强烈抑制菌丝伸长。碘化丙啶摄取试验表明,Vv-AMP 1的抑制活性可能与改变真菌膜的膜渗透性有关。一个浆果特异性的cDNA克隆,Vv-AMP 1,分离和表征,并显示编码植物防御素。重组Vv-AMP 1显示对广谱真菌的非形态发生性抗真菌活性,可能改变了真菌病原体的膜通透性。这种肽的表达在葡萄属葡萄中受到高度调节,暗示在浆果成熟过程中具有重要的防御作用。
Latest research shows that small antimicrobial peptides play a role in the innate defense system of plants. These peptides typically contribute to preformed defense by developing protective barriers around germinating seeds or between different tissue layers within plant organs. The encoding genes could also be upregulated by abiotic and biotic stimuli during active defense processes. The peptides display a broad spectrum of antimicrobial activities. Their potent anti-pathogenic characteristics have ensured that they are promising targets in the medical and agricultural biotechnology sectors. A berry specific cDNA sequence designated Vv-AMP1, Vitis vinifera antimicrobial peptide 1, was isolated from Vitis vinifera. Vv-AMP1 encodes for a 77 amino acid peptide that shows sequence homology to the family of plant defensins. Vv-AMP1 is expressed in a tissue specific, developmentally regulated manner, being only expressed in berry tissue at the onset of berry ripening and onwards. Treatment of leaf and berry tissue with biotic or abiotic factors did not lead to increased expression of Vv-AMP1 under the conditions tested. The predicted signal peptide of Vv-AMP1, fused to the green fluorescent protein (GFP), showed that the signal peptide allowed accumulation of its product in the apoplast. Vv-AMP1 peptide, produced in Escherichia coli, had a molecular mass of 5.495 kDa as determined by mass spectrometry. Recombinant Vv-AMP1 was extremely heat-stable and showed strong antifungal activity against a broad spectrum of plant pathogenic fungi, with very high levels of activity against the wilting disease causing pathogens Fusarium oxysporum and Verticillium dahliae. The Vv-AMP1 peptide did not induce morphological changes on the treated fungal hyphae, but instead strongly inhibited hyphal elongation. A propidium iodide uptake assay suggested that the inhibitory activity of Vv-AMP1 might be associated with altering the membrane permeability of the fungal membranes. A berry specific cDNA clone, Vv-AMP1, was isolated and characterized and shown to encode a plant defensin. Recombinant Vv-AMP1 displayed non-morphogenic antifungal activity against a broad spectrum of fungi, probably altering the membrane permeability of the fungal pathogens. The expression of this peptide is highly regulated in Vitis vinifera, hinting at an important defense role during berry-ripening.
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发表时间: 2000-06-15
影响因子: 3.9
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发表时间: 1990-05-01
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