New Antibacterial Peptides from the Freshwater Mollusk Pomacea poeyana (Pilsbry, 1927).
New Antibacterial Peptides from the Freshwater Mollusk Pomacea poeyana (Pilsbry, 1927).
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DOI：
10.3390/biom10111473
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发表时间：
2020-10-23
期刊：
影响因子：
5.5
通讯作者：
Otero-González A
中科院分区：
文献类型：
--
作者：
González García M;Rodríguez A;Alba A;Vázquez AA;Morales Vicente FE;Pérez-Erviti J;Spellerberg B;Stenger S;Grieshober M;Conzelmann C;Münch J;Raber H;Kubiczek D;Rosenau F;Wiese S;Ständker L;Otero-González A
抗菌肽（Antimicrobial Peptides，AMP）是一类对多种病原体具有抗菌活性的生物分子。在过去的几十年中，AMP已经代表了治疗感染性疾病的重要替代方案。它们与自然资源的隔离已经得到了广泛的研究。从这个意义上说，软体动物是有前途的生物体，因为它们的免疫系统主要依赖于先天性反应。在这份报告中，我们表征了古巴淡水蜗牛Pomacea poeyana（Pilsbry，1927）的肽级分，并通过nanoLC-ESI-MS-MS技术鉴定了37种不同的肽。从这些肽序列中，使用生物信息学预测工具，我们发现了两个潜在的抗菌肽，命名为Pom-1（KCAGSIAWAIGSGLFGGAKLIKKYIAELGGLQ）和Pom-2（KEIERAGQRIRDAIISAAPAVETLAQAQKIIKGG）。数据库检索显示，Pom-1是以前从细菌酪丁酸梭菌中分离的梭菌素574的片段，Pom-2是首先从大蜡螟血淋巴中分离的天蚕素D样肽的片段。这些序列是化学合成的，并针对不同的人类病原体进行评估。有趣的是，在胶束存在下对这两种肽的结构预测显示了包含由短环连接的两个α螺旋的模型。对Pom-1和Pom-2在水中的圆二色光谱分析表明，这两种结构都含有较高的无规卷曲含量、一定含量的α-螺旋和较低的β-折叠含量。与其他描述的AMP在水中显示无序结构一样，肽在细菌膜存在下可以采用螺旋构象。在抗微生物测定中，Pom-1表现出对革兰氏阴性菌铜绿假单胞菌的高活性和对肺炎克雷伯氏菌和单核细胞增生李斯特菌的中等活性。两种肽均未显示抗真菌作用。Pom-1在体外适度抑制寨卡病毒感染，但轻微增强HIV-1感染。对原代人巨噬细胞的细胞毒性评价未显示对THP-1细胞的毒性，尽管在高浓度的Pom-1中观察到轻微的总体毒性。我们假设这两种肽可能在P. poeyana的先天防御中发挥关键作用，并代表了有希望的人类抗菌候选物。
Antimicrobial peptides (AMPs) are biomolecules with antimicrobial activity against a broad group of pathogens. In the past few decades, AMPs have represented an important alternative for the treatment of infectious diseases. Their isolation from natural sources has been widely investigated. In this sense, mollusks are promising organisms for the identification of AMPs given that their immune system mainly relies on innate response. In this report, we characterized the peptide fraction of the Cuban freshwater snail Pomacea poeyana (Pilsbry, 1927) and identified 37 different peptides by nanoLC-ESI-MS-MS technology. From these peptide sequences, using bioinformatic prediction tools, we discovered two potential antimicrobial peptides named Pom-1 (KCAGSIAWAIGSGLFGGAKLIKIKKYIAELGGLQ) and Pom-2 (KEIERAGQRIRDAIISAAPAVETLAQAQKIIKGG). Database search revealed that Pom-1 is a fragment of Closticin 574 previously isolated from the bacteria Clostridium tyrobutyrium, and Pom-2 is a fragment of cecropin D-like peptide first isolated from Galleria mellonella hemolymph. These sequences were chemically synthesized and evaluated against different human pathogens. Interestingly, structural predictions of both peptides in the presence of micelles showed models that comprise two alpha helices joined by a short loop. The CD spectra analysis of Pom-1 and Pom-2 in water showed for both structures a high random coil content, a certain content of α-helix and a low β-sheet content. Like other described AMPs displaying a disordered structure in water, the peptides may adopt a helical conformation in presence of bacterial membranes. In antimicrobial assays, Pom-1 demonstrated high activity against the Gram-negative bacteria Pseudomonas aeruginosa and moderate activity against Klebsiella pneumoniae and Listeria monocytogenes. Neither of the two peptides showed antifungal action. Pom-1 moderately inhibits Zika Virus infection but slightly enhances HIV-1 infectivion in vitro. The evaluation of cell toxicity on primary human macrophages did not show toxicity on THP-1 cells, although slight overall toxicity was observed in high concentrations of Pom-1. We assume that both peptides may play a key role in innate defense of P. poeyana and represent promising antimicrobial candidates for humans.
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影响因子：
4
作者：
Lambert, RJW;Pearson, J
通讯作者：
Pearson, J
影响因子：
4.4
作者：
Cox, Juergen;Neuhauser, Nadin;Mann, Matthias
通讯作者：
Mann, Matthias
DOI：
10.1111/j.1432-1033.1993.tb18287.x
发表时间：
1993-10-15
期刊：
EUROPEAN JOURNAL OF BIOCHEMISTRY
影响因子：
--
作者：
IWAI, H;NAKAJIMA, Y;SHIMADA, I
通讯作者：
SHIMADA, I
影响因子：
5.2
作者：
Guilhelmelli F;Vilela N;Albuquerque P;Derengowski Lda S;Silva-Pereira I;Kyaw CM
通讯作者：
Kyaw CM
影响因子：
8
作者：
BECHINGER, B;ZASLOFF, M;OPELLA, SJ
通讯作者：
OPELLA, SJ