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Identification and Structural Characterization of a Broadly Neutralizing Antibody Targeting a Novel Conserved Epitope on the Influenza Virus H5N1 Hemagglutinin 期刊论文

编号：

bbd51fe9-98ee-49ec-86f4-8b33a62f2a9f
作者：

Du, Lanying^[1];Jin, Lei^[2];Zhao, Guangyu^[3];Sun, Shihui^[3];Li, Junfeng^[3];Yu, Hong^[3];Li, Ye^[1];Zheng, BoJian^[4];Liddington, Robert C.^[2];Zhou, Yusen^[3];Jiang, Shibo(姜世勃)^[1,5,6,7]
语种：

English
期刊：

JOURNAL OF VIROLOGY ISSN：0022-538X 2013 年 87 卷 4 期 (2215 - 2225) ; FEB
收录：
摘要：

The unabated circulation of the highly pathogenic avian influenza A virus/H5N1 continues to be a serious threat to public health worldwide. Because of the high frequency of naturally occurring mutations, the emergence of H5N1 variants with high virulence has raised great concerns about the potential transmissibility of the virus in humans. Recent studies have shown that laboratory-mutated or reassortant H5N1 viruses could be efficiently transmitted among mammals, particularly ferrets, the best animal model for humans. Thus, it is critical to establish effective strategies to combat future H5N1 pandemics. In this study, we identified a broadly neutralizing monoclonal antibody (MAb), HA-7, that potently neutralized all tested strains of H5N1 covering clades 0, 1, 2.2, 2.3.4, and 2.3.2.1 and completely protected mice against lethal challenges of H5N1 viruses from clades 1 and 2.3.4. HA-7 specifically targeted the globular head of the H5N1 virus hemagglutinin (HA). Using electron microscopy technology with three-dimensional reconstruction (3D-EM), we discovered that HA-7 bound to a novel and highly conserved conformational epitope that was centered on residues 81 to 83 and 117 to 122 of HA1 (H5 numbering). We further demonstrated that HA-7 inhibited viral entry during postattachment events but not at the receptor-binding step, which is fully consistent with the 3D-EM result. Taken together, we propose that HA-7 could be humanized as an effective passive immunotherapeutic agent for antiviral stockpiling for future influenza pandemics caused by emerging unpredictable H5N1 strains. Our study also provides a sound foundation for the rational design of vaccines capable of inducing broad-spectrum immunity against H5N1.
推荐引用方式
GB/T 7714：

Du Lanying,Jin Lei,Zhao Guangyu, et al. Identification and Structural Characterization of a Broadly Neutralizing Antibody Targeting a Novel Conserved Epitope on the Influenza Virus H5N1 Hemagglutinin [J].JOURNAL OF VIROLOGY,2013,87(4):2215-2225.
APA：

Du Lanying,Jin Lei,Zhao Guangyu,Sun Shihui,&Jiang Shibo.(2013).Identification and Structural Characterization of a Broadly Neutralizing Antibody Targeting a Novel Conserved Epitope on the Influenza Virus H5N1 Hemagglutinin .JOURNAL OF VIROLOGY,87(4):2215-2225.
MLA：

Du Lanying, et al. "Identification and Structural Characterization of a Broadly Neutralizing Antibody Targeting a Novel Conserved Epitope on the Influenza Virus H5N1 Hemagglutinin" .JOURNAL OF VIROLOGY 87,4(2013):2215-2225.

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