Henrique Nemésio, M Francisca Palomares-Jerez, José Villalaín
{"title":"登革病毒C蛋白疏水片段。与模型膜的相互作用。","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":"{\"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}","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}
Hydrophobic segment of dengue virus C protein. Interaction with model membranes.
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.
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.
求助内容：
应助结果提醒方式：
京公网安备 11010802042870号
