کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8327198 | 1540198 | 2018 | 38 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Intrinsic structural versatility of the highly conserved 412-423 epitope of the Hepatitis C Virus E2 protein
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کلمات کلیدی
RMSDPDBmAbCD81Protein flexibility - انعطاف پذیری پروتئینThT - بلهThioflavin T - تیوفلاوین Tcluster of differentiation 81 - خوشه تمایز 81Molecular dynamics - دینامیک ملکولی یا پویایی مولکولیReplica exchange molecular dynamics - دینامیک مولکولی مبادله ی ReplicaFab - فابantigen-binding fragment - قطعه اتصال آنتی ژنroot mean square deviation - میانگین انحراف مربع ریشهHepatitis C virus - هپاتیت سیHCV - هپاتیت سیMonoclonal antibodies - پادتنهای تَکتیرهProtein Data Bank - پروتئین بانک اطلاعاتی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
HCV infection is a major threaten for human health as it affects hundreds of million people worldwide. Here we investigated the conformational properties of the 412-423 fragment of the envelope E2 protein, one of the most immunogenic regions of the virus proteome whose characterization may provide interesting insights for anti-HCV vaccine development. The spectroscopic characterization of the polypeptide unravels its unexpected tendency to form amyloid-like aggregates. When kept in monomeric state, it shows a limited tendency to adopt regular secondary structure. Enhanced molecular dynamics simulations, starting from four distinct conformational states, highlight its structural versatility. Interestingly, all multiform conformational states of the polypeptide detected in crystallographic complexes with antibodies are present in the structural ensemble of all simulations. This observation corroborates the idea that known antibodies recognize this region through a conformational selection mechanism. Accordingly, the design of effective anti-HCV vaccines should consider the intrinsic flexibility of this region. The structural versatility of the 412-423 region is particularly puzzling if its remarkable sequence conservation is considered. It is likely that flexibility and sequence conservation are important features that endow this epitope with the ability to accomplish distinct functions such as immunity escape and interaction with host receptors.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 116, September 2018, Pages 620-632
Journal: International Journal of Biological Macromolecules - Volume 116, September 2018, Pages 620-632
نویسندگان
Nicole Balasco, Daniela Barone, Emanuela Iaccarino, Annamaria Sandomenico, Alfonso De Simone, Menotti Ruvo, Luigi Vitagliano,