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| DOI | 10.1126/science.aam7260 |
| Structural basis for antibody-mediated neutralization of Lassa virus | |
| Hastie K.M.; Zandonatti M.A.; Kleinfelter L.M.; Heinrich M.L.; Rowland M.M.; Chandran K.; Branco L.M.; Robinson J.E.; Garry R.F.; Saphire E.O. | |
| 发表日期 | 2017 |
| ISSN | 0036-8075 |
| 起始页码 | 923 |
| 结束页码 | 928 |
| 卷号 | 356期号:6341 |
| 英文摘要 | The arenavirus Lassa causes severe hemorrhagic fever and a significant disease burden in West Africa every year. The glycoprotein, GPC, is the sole antigen expressed on the viral surface and the critical target for antibody-mediated neutralization. Here we present the crystal structure of the trimeric, prefusion ectodomain of Lassa GP bound to a neutralizing antibody from a human survivor at 3.2-angstrom resolution. The antibody extensively anchors two monomers together at the base of the trimer, and biochemical analysis suggests that it neutralizes by inhibiting conformational changes required for entry. This work illuminates pH-driven conformational changes in both receptor-binding and fusion subunits of Lassa virus, illustrates the unique assembly of the arenavirus glycoprotein spike, and provides a much-needed template for vaccine design against these threats to global health. Copyright 2016 by the American Association for the Advancement of Science; all rights reserved. |
| 英文关键词 | epitope; glycoprotein; monomer; neutralizing antibody; viral protein; virus antibody; virus antigen; epitope; neutralizing antibody; protein binding; virus antibody; virus envelope protein; antibody; antigen; biochemical composition; disease incidence; neutralization; protein; public health; vaccine; virus; amino terminal sequence; antibody structure; antigen binding; Article; biochemical analysis; carboxy terminal sequence; conformational transition; crystal structure; gene fusion; human; Lassa virus; New World arenavirus; nonhuman; priority journal; protein assembly; receptor binding; structure analysis; virion; virus neutralization; virus viability; chemistry; crystallization; immunology; Lassa fever; Lassa virus; metabolism; molecular model; pH; physiology; protein conformation; protein multimerization; protein quaternary structure; protein stability; virology; virus entry; West Africa; Arenavirus; Lassa virus; Antibodies, Neutralizing; Antibodies, Viral; Crystallization; Epitopes; Humans; Hydrogen-Ion Concentration; Lassa Fever; Lassa virus; Models, Molecular; Protein Binding; Protein Conformation; Protein Multimerization; Protein Stability; Protein Structure, Quaternary; Viral Envelope Proteins; Virus Internalization |
| 语种 | 英语 |
| 来源期刊 | Science
 |
| 文献类型 | 期刊论文 |
| 条目标识符 | http://gcip.llas.ac.cn/handle/2XKMVOVA/243970 |
| 作者单位 | Department of Immunology and Microbial Science, Scripps Research Institute, San Diego, CA 92037, United States; Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY, United States; Zalgen Labs, Germantown, MD, United States; Department of Pediatrics, School of Medicine, Tulane University, New Orleans, LA, United States; Department of Microbiology and Immunology, Tulane University, New Orleans, LA, United States; Skaggs Institute for Chemical Biology, Scripps Research Institute, San Diego, CA, United States |
| 推荐引用方式 GB/T 7714 | Hastie K.M.,Zandonatti M.A.,Kleinfelter L.M.,et al. Structural basis for antibody-mediated neutralization of Lassa virus[J],2017,356(6341). |
| APA | Hastie K.M..,Zandonatti M.A..,Kleinfelter L.M..,Heinrich M.L..,Rowland M.M..,...&Saphire E.O..(2017).Structural basis for antibody-mediated neutralization of Lassa virus.Science,356(6341). |
| MLA | Hastie K.M.,et al."Structural basis for antibody-mediated neutralization of Lassa virus".Science 356.6341(2017). |
| 条目包含的文件 | 条目无相关文件。 | |||||
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