https://scholars.lib.ntu.edu.tw/handle/123456789/405056
標題: | Extended low-resolution structure of a leptospira antigen offers high bactericidal antibody accessibility amenable to vaccine design | 作者: | CHING-LIN HSIEH Ptak, Christopher P. Tseng, Andrew de Souza Suguiura, Igor Massahiro McDonough, Sean P. Sritrakul, Tepyuda Li, Ting YI-PIN LIN Gillilan, Richard E. Oswald, Robert E. Chang, Yung Fu CHING-LIN HSIEH Ptak, Christopher P. Tseng, Andrew de Souza Suguiura, Igor Massahiro McDonough, Sean P. Sritrakul, Tepyuda Li, Ting Gillilan, Richard E. Oswald, Robert E. Chang, Yung Fu |
公開日期: | 6-十二月-2017 | 卷: | 6 | 期: | 4 | 起(迄)頁: | e30051 | 來源出版物: | eLife | 摘要: | © Hsieh et al. Pathogens rely on proteins embedded on their surface to perform tasks essential for host infection. These obligatory structures exposed to the host immune system provide important targets for rational vaccine design. Here, we use a systematically designed series of multi-domain constructs in combination with small angle X-ray scattering (SAXS) to determine the structure of the main immunoreactive region from a major antigen from Leptospira interrogans, LigB. An anti- LigB monoclonal antibody library exhibits cell binding and bactericidal activity with extensive domain coverage complementing the elongated architecture observed in the SAXS structure. Combining antigenic motifs in a single-domain chimeric immunoglobulin-like fold generated a vaccine that greatly enhances leptospiral protection over vaccination with single parent domains. Our study demonstrates how understanding an antigen’s structure and antibody accessible surfaces can guide the design and engineering of improved recombinant antigen-based vaccines. |
URI: | https://scholars.lib.ntu.edu.tw/handle/123456789/405056 | ISSN: | 0006-291X | DOI: | 10.7554/eLife.30051 |
顯示於: | 職能治療學系 |
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