Host protein inhibits influenza virus replication mystery
January 26, 2018 Source: Science and Technology Daily
Window._bd_share_config={ "common":{ "bdSnsKey":{ },"bdText":"","bdMini":"2","bdMiniList":false,"bdPic":"","bdStyle":" 0","bdSize":"16"},"share":{ }};with(document)0[(getElementsByTagName('head')[0]||body).appendChild(createElement('script')) .src='http://bdimg.share.baidu.com/static/api/js/share.js?v=89860593.js?cdnversion='+~(-new Date()/36e5)];According to the latest news from the Chinese Academy of Agricultural Sciences, the National Avian Influenza Reference Laboratory of the Harbin Veterinary Research Institute of the hospital has devoted research to the mechanism of host protein regulation of influenza virus replication cycle and made breakthroughs, further improving the interaction network between influenza virus and host protein. It has deepened the understanding of the replication cycle of influenza virus and provided a potential target for the development of new anti-influenza drugs. Related research results have recently been published online in the International Journal of Pathogens, the "Public Science Library Pathogens".
According to reports, the flu virus has evolved and mutated, posing a constant threat to animal and human health, and may trigger new animal outbreaks and public health crises at any time. In-depth study of the pathogenesis of influenza virus, found that the host protein interacting with the virus replication process, revealing its mechanism involved in the regulation of viral replication cycle, can provide a theoretical basis for the development of new anti-influenza drugs and intervention therapy.
The laboratory doctoral student Luo Weiyu and master student Zhang Jie, under the guidance of Li Chengjun, Associate Professor Jiang Li and Associate Professor Chen Hualan, screened the host protein phospholipid crawling enzyme 1 (PLSCR1), which interacted directly with influenza virus NP protein, and found that PLSCR1 passed NP protein binding inhibits the entry of NP and viral ribonucleoprotein complex (vRNP) into the nucleus, delaying the entire replication cycle of the virus, and thus significantly inhibiting the proliferation of influenza virus. Further studies have found that PLSCR1, NP and import protein α (Importin α) form a trimer, which blocks the binding of the key factor input protein β (Importin β) to Importin α, and prevents the combination of influenza virus NP and vRNP. The body enters the nucleus through an active input pathway, thereby inhibiting influenza virus replication. (Reporter Yan Jian)
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