التفاصيل البيبلوغرافية
| العنوان: |
HCV E2 core structures and mAbs: something is still missing |
| المؤلفون: |
Jennifer M. Pfaff, Giuseppe A. Sautto, Trevor Barnes, Matteo Dal Peraro, Roberto Burioni, Nicasio Mancini, Nicola Clementi, Kristen M. Kahle, Matteo Castelli, Benjamin J. Doranz, Massimo Clementi |
| المساهمون: |
Castelli, M, Clementi, Nicola, Sautto, Ga, Pfaff, J, Kahle, Km, Barnes, T, Doranz, Bj, Dal Peraro, M, Clementi, Massimo, Burioni, Roberto, Mancini, Nicasio, Castelli, Matteo |
| المصدر: |
Drug discovery today |
| سنة النشر: |
2014 |
| مصطلحات موضوعية: |
Pharmacology, Models, Molecular, 0303 health sciences, Chemistry, Protein Conformation, 030302 biochemistry & molecular biology, Disulfide bond, Antibodies, Monoclonal, Computational biology, Hepacivirus, Virology, Article, 3. Good health, 03 medical and health sciences, Protein structure, Viral Envelope Proteins, Antibodies monoclonal, Drug Discovery, Animals, Humans, Functional studies, Cysteine, Disulfides, 030304 developmental biology |
| الوصف: |
The lack of structural information on hepatitis C virus (HCV) surface proteins has so far hampered the development of effective vaccines. Recently, two crystallographic structures have described the core portion (E2c) of E2 surface glycoprotein, the primary mediator of HCV entry. Despite the importance of these studies, the E2 overall structure is still unknown and, most importantly, several biochemical and functional studies are in disagreement with E2c structures. Here, the main literature will be discussed and an alternative disulfide bridge pattern will be proposed, based on unpublished human monoclonal antibody reactivity. A modeling strategy aiming at recapitulating the available structural and functional studies of E2 will also be proposed. © 2014 Elsevier Ltd. The lack of structural information on hepatitis C virus (HCV) surface proteins has so far hampered the development of effective vaccines. Recently, two crystallographic structures have described the core portion (E2c) of E2 surface glycoprotein, the primary mediator of HCV entry. Despite the importance of these studies, the E2 overall structure is still unknown and, most importantly, several biochemical and functional studies are in disagreement with E2c structures. Here, the main literature will be discussed and an alternative disulfide bridge pattern will be proposed, based on unpublished human monoclonal antibody reactivity. A modeling strategy aiming at recapitulating the available structural and functional studies of E2 will also be proposed. |
| اللغة: |
English |
| URL الوصول: |
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82e46dced9fd93b1f433b2a86515cd90
https://europepmc.org/articles/PMC4706463/ |
| Rights: |
OPEN |
| رقم الانضمام: |
edsair.doi.dedup.....82e46dced9fd93b1f433b2a86515cd90 |
| قاعدة البيانات: |
OpenAIRE |