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-Structure paper
タイトル | The C-Terminal Arm of the Human Papillomavirus Major Capsid Protein Is Immunogenic and Involved in Virus-Host Interaction. |
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ジャーナル・号・ページ | Structure, Vol. 24, Issue 6, Page 874-885, Year 2016 |
掲載日 | 2016年6月7日 |
著者 | Zhihai Li / Xiaodong Yan / Hai Yu / Daning Wang / Shuo Song / Yunbing Li / Maozhou He / Qiyang Hong / Qingbing Zheng / Qinjian Zhao / Ying Gu / Jun Zhang / Mandy E W Janssen / Giovanni Cardone / Norman H Olson / Timothy S Baker / Shaowei Li / Ningshao Xia / |
PubMed 要旨 | Cervical cancer is the second most prevalent malignant tumor among women worldwide. High-risk human papillomaviruses (HPVs) are believed to be the major causative pathogens of mucosal epithelial ...Cervical cancer is the second most prevalent malignant tumor among women worldwide. High-risk human papillomaviruses (HPVs) are believed to be the major causative pathogens of mucosal epithelial cancers including cervical cancer. The HPV capsid is made up of 360 copies of major (L1) and 72 copies of minor (L2) capsid proteins. To date, limited high-resolution structural information about the HPV capsid has hindered attempts to understand details concerning the mechanisms by which HPV assembles and infects cells. In this study, we have constructed a pseudo-atomic model of the HPV59 L1-only capsid and demonstrate that the C-terminal arm of L1 participates in virus-host interactions. Moreover, when conjugated to a scaffold protein, keyhole limpet hemocyanin (KLH), this arm is immunogenic in vivo. These results provide new insights that will help elucidate HPV biology, and hence pave a way for the design of next-generation HPV vaccines. |
リンク | Structure / PubMed:27276427 / PubMed Central |
手法 | EM (単粒子) / X線回折 |
解像度 | 4.011 - 6.0 Å |
構造データ | EMDB-8147: Cryo-EM structure of Human Papillomavirus Type 59 L1 Virus-like Particle PDB-5j6r: |
由来 |
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キーワード | VIRAL PROTEIN / Major structural protein / Pentamer / VIRUS / Capsid / T=7 icosahedral / Virus-like Particle |