Hydrophobic segment of dengue virus C protein. Interaction with model membranes.

Q3 Biochemistry, Genetics and Molecular Biology

Molecular Membrane Biology Pub Date : 2013-07-01 Epub Date: 2013-06-07 DOI:10.3109/09687688.2013.805835

Henrique Nemésio, M Francisca Palomares-Jerez, José Villalaín

{"title":"Hydrophobic segment of dengue virus C protein. Interaction with model membranes.","authors":"Henrique Nemésio, M Francisca Palomares-Jerez, José Villalaín","doi":"10.3109/09687688.2013.805835","DOIUrl":null,"url":null,"abstract":"<p><p>Dengue virus (DENV) C protein is essential for viral assembly. DENV C protein associates with intracellular membranes through a conserved hydrophobic domain and accumulates around endoplasmic reticulum-derived lipid droplets which could provide a platform for capsid formation during assembly. In a previous work we described a region in DENV C protein which induced a nearly complete membrane rupture of several membrane model systems, which was coincident with the theoretically predicted highly hydrophobic region of the protein. In this work we have carried out a study of the binding to and interaction with model biomembranes of a peptide corresponding to this DENV C region, DENV2C6. We show that DENV2C6 partitions into phospholipid membranes, is capable of rupturing membranes even at very low peptide-to-lipid ratios and its membrane-activity is modulated by lipid composition. These results identify an important region in the DENV C protein which might be directly implicated in the DENV life cycle through the modulation of membrane structure.</p>","PeriodicalId":18858,"journal":{"name":"Molecular Membrane Biology","volume":"30 4","pages":"273-87"},"PeriodicalIF":0.0000,"publicationDate":"2013-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/09687688.2013.805835","citationCount":"14","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Molecular Membrane Biology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3109/09687688.2013.805835","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2013/6/7 0:00:00","PubModel":"Epub","JCR":"Q3","JCRName":"Biochemistry, Genetics and Molecular Biology","Score":null,"Total":0}

引用次数: 14

Abstract

Dengue virus (DENV) C protein is essential for viral assembly. DENV C protein associates with intracellular membranes through a conserved hydrophobic domain and accumulates around endoplasmic reticulum-derived lipid droplets which could provide a platform for capsid formation during assembly. In a previous work we described a region in DENV C protein which induced a nearly complete membrane rupture of several membrane model systems, which was coincident with the theoretically predicted highly hydrophobic region of the protein. In this work we have carried out a study of the binding to and interaction with model biomembranes of a peptide corresponding to this DENV C region, DENV2C6. We show that DENV2C6 partitions into phospholipid membranes, is capable of rupturing membranes even at very low peptide-to-lipid ratios and its membrane-activity is modulated by lipid composition. These results identify an important region in the DENV C protein which might be directly implicated in the DENV life cycle through the modulation of membrane structure.

查看原文本刊更多论文

登革病毒C蛋白疏水片段。与模型膜的相互作用。

登革病毒(DENV) C蛋白是病毒组装所必需的。denvc蛋白通过保守的疏水结构域与细胞膜结合，并在内质网衍生的脂滴周围积聚，为组装过程中衣壳的形成提供了平台。在之前的工作中，我们描述了DENV C蛋白中的一个区域，该区域诱导了几个膜模型系统的几乎完全的膜破裂，这与理论预测的蛋白质高度疏水区域一致。在这项工作中，我们研究了DENV2C6对应的denvc区域肽与模型生物膜的结合和相互作用。我们发现，DENV2C6分裂成磷脂膜，即使在非常低的肽脂比下也能破裂膜，其膜活性受到脂质组成的调节。这些结果确定了DENV C蛋白中的一个重要区域，该区域可能通过调节膜结构直接参与DENV生命周期。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

求助全文

约1分钟内获得全文求助全文

来源期刊

Molecular Membrane Biology 生物-生化与分子生物学

CiteScore

4.80

自引率

0.00%

发文量

审稿时长

>12 weeks

期刊介绍： Cessation. Molecular Membrane Biology provides a forum for high quality research that serves to advance knowledge in molecular aspects of biological membrane structure and function. The journal welcomes submissions of original research papers and reviews in the following areas: • Membrane receptors and signalling • Membrane transporters, pores and channels • Synthesis and structure of membrane proteins • Membrane translocation and targeting • Lipid organisation and asymmetry • Model membranes • Membrane trafficking • Cytoskeletal and extracellular membrane interactions • Cell adhesion and intercellular interactions • Molecular dynamics and molecular modelling of membranes. • Antimicrobial peptides.