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Virucidal activity of human α- and β-defensins against hepatitis C virus genotype 4

机译：人类α-防御素和β-防御素对丙型肝炎病毒基因型4的杀病毒活性

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摘要

Hepatitis C virus (HCV) is the major etiological agent of human non-A and non-B hepatitis affecting about 180 million people worldwide. The goal of the current study was to find effective anti-HCV proteins. As a result defensins were selected as promising candidates due to their well-known anti-viral potential and small size. We conducted in vitro evaluation of two kinds of defensins (human α- and β-defensins and synthetic linear avian α-defensins) using tissue culture combined with reverse transcription nested PCR (RT-nested-PCR) and real-time PCR. Human α- and β-defensins showed strong anti-HCV activity in experiments on cellular protection, neutralization, and treatment at all concentrations used (10, 20 and 50 μg). The synthetic linear defensins could reach similar anti-HCV potential only at a noticeably higher concentration (250 μg) and do not show noticeable activity at 10 and 20 μg. This study suggests that defensins are potent anti-HCV agents.
机译：丙型肝炎病毒（HCV）是人类非甲型和非乙型肝炎的主要病原体，影响着全世界约1.8亿人。当前研究的目的是找到有效的抗HCV蛋白。结果，防御素由于其众所周知的抗病毒潜力和小尺寸而被选为有前途的候选药物。我们使用组织培养结合逆转录巢式PCR（RT-nested-PCR）和实时PCR进行了两种防御素（人α-防御素和β-防御素以及合成的线性禽类α-防御素）的体外评估。人α-防御素和β-防御素在所有使用浓度（10、20和50μg）的细胞保护，中和和治疗实验中均显示出强大的抗HCV活性。合成的线性防御素只有在明显更高的浓度（250μg）时才能达到相似的抗HCV潜力，而在10和20μg时未显示出明显的活性。这项研究表明防御素是有效的抗HCV药物。

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  • 来源
    《Molecular BioSystems》 |2016年第9期|2785-2797|共13页
  • 作者

    Ehab H. Mattar; Hussein A. Almehdar; Vladimir N. Uversky; Elrashdy M. Redwan;

  • 作者单位

    Department of Biological Sciences, Faculty of Sciences, King Abdulaziz University, P.O. Box 80203, Jeddah, Saudi Arabia;

    Department of Biological Sciences, Faculty of Sciences, King Abdulaziz University, P.O. Box 80203, Jeddah, Saudi Arabia;

    Department of Biological Sciences, Faculty of Sciences, King Abdulaziz University, P.O. Box 80203, Jeddah, Saudi Arabia,Department of Molecular Medicine and USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, USA,Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, St. Petersburg, Russian Federation;

    Department of Biological Sciences, Faculty of Sciences, King Abdulaziz University, P.O. Box 80203, Jeddah, Saudi Arabia,Therapeutic and Protective Proteins Laboratory, Protein Research Department, Genetic Engineering and Biotechnology Research Institute, City for Scientific Research and Technology Applications, New Borg EL-Arab 21934, Alexandria, Egypt;

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