Iga targeting on the alpha-molecular recognition element (alpha-more) of viral phosphoprotein inhibits measles virus replication by interrupting formation and function of p-n complex intracellularly
文献类型：期刊论文
| 作者 | Zhou, Dihan1,2; Yang, Yi1,3; Zhao, Bali1,3; Yu, Jie1,3; Cao, Yuan1,3; Yan, Hu1,3; Zhao, Wei1,3; Chen, Longyun4,5; Chen, Fang2; Li, Xiaodan2 |
| 刊名 | Antiviral research
 |
| 出版日期 | 2018 |
| 卷号 | 161页码:144-153 |
| 关键词 | Iga Measles virus Viral phosphoprotein Alpha-molecular recognition element Intracellular neutralization P-n complex |
| ISSN号 | 0166-3542 |
| DOI | 10.1016/j.antiviral.2018.11.014 |
| 通讯作者 | Deng, li(drdengli@126.com) ; Yan, huimin(hmyan@wh.iov.cn) |
| 英文摘要 | Secretory iga (siga) antibody is unique for its capability to transit through epithelial cells by transcytosis and thus has opportunities and probabilities to interact with all viral components during viral replication which may result in the inhibition of viral replication intracellularly. here, we report a novel iga mab 1d11-iga against phosphoprotein (p) of measles virus (mv), which is able to interact specifically with p in mv infected vero-pigr cells grown in a two-chamber transwell system. the binding epitope of 1d11-iga involves a key residue proline 23 in p protein, which is among the alpha-molecular recognition element (alpha-more) of p and critical for n-0-p complex. the antibody appears to block p to interact with n in p-n complex and thus may inhibit the function of viral rdrp complex, which results in decreased synthesis of viral genome rna and mrna. our data together demonstrate that iga is able to interact with viral phosphoprotein intraepithelial cells and neutralize viral replication by interrupting formation of p-n complex and function of rdrp. the findings highlight that iga has a unique anti-viral activity by targeting viral conserved components critical for viral replication, which serves as a proof-of-concept assessment of the druggability of mononegavirales p-n interfaces. |
| WOS关键词 | C-TERMINAL DOMAIN ; IMMUNOGLOBULIN-A ; NUCLEOCAPSID PROTEIN ; STRUCTURAL DISORDER ; CRYSTAL-STRUCTURE ; NUCLEOPROTEIN ; BINDING ; SENDAI ; NEUTRALIZATION ; ANTIBODIES |
| WOS研究方向 | Pharmacology & Pharmacy ; Virology |
| WOS类目 | Pharmacology & Pharmacy ; Virology |
| 语种 | 英语 |
| WOS记录号 | WOS:000456900100017 |
| 出版者 | ELSEVIER SCIENCE BV |
| URI标识 | http://www.irgrid.ac.cn/handle/1471x/2373197 |
| 专题 | 武汉病毒研究所 |
| 通讯作者 | Deng, Li; Yan, Huimin |
| 作者单位 | 1.Chinese Acad Sci, Wuhan Inst Virol, State Key Lab Virol, Mucosal Immun Res Grp, Wuhan 430071, Hubei, Peoples R China 2.Guangzhou Women & Children Med Ctr, Guangzhou Inst Pediat, Guangzhou 510623, Guangdong, Peoples R China 3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 4.Wuhan Univ, Coll Life Sci, State Key Lab Virol, Wuhan 430072, Hubei, Peoples R China 5.Wuhan Univ, Coll Life Sci, Modern Virol Res Ctr, Wuhan 430072, Hubei, Peoples R China |
| 推荐引用方式 GB/T 7714 | Zhou, Dihan,Yang, Yi,Zhao, Bali,et al. Iga targeting on the alpha-molecular recognition element (alpha-more) of viral phosphoprotein inhibits measles virus replication by interrupting formation and function of p-n complex intracellularly[J]. Antiviral research,2018,161:144-153. |
| APA | Zhou, Dihan.,Yang, Yi.,Zhao, Bali.,Yu, Jie.,Cao, Yuan.,...&Yan, Huimin.(2018).Iga targeting on the alpha-molecular recognition element (alpha-more) of viral phosphoprotein inhibits measles virus replication by interrupting formation and function of p-n complex intracellularly.Antiviral research,161,144-153. |
| MLA | Zhou, Dihan,et al."Iga targeting on the alpha-molecular recognition element (alpha-more) of viral phosphoprotein inhibits measles virus replication by interrupting formation and function of p-n complex intracellularly".Antiviral research 161(2018):144-153. |
入库方式： iSwitch采集
来源：武汉病毒研究所
浏览0
下载0
收藏0
其他版本
除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。