Scientists have discovered a negative regulatory protein of Ebola virus in humans
January 03, 2019 Source: Ministry of Science and Technology
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)];Recently, American scientists published a research paper entitled "Protein Interaction Mapping Identifies RBBP6 as a Negative Regulator of Ebola Virus Replication" online in Cell (IF=31.398). This paper identifies RBBP6 as a negative regulator of Ebola replication through protein interaction mapping.
Ebola virus (EBOV) belongs to the family filoviridae, which is mainly transmitted through the blood and excretion of patients. After the patient is infected, it will cause an acute hemorrhagic infection. The virus is in the shape of a linear body of different lengths, and the inner 1 contains an inner spiral shell with a diameter of 40 nm, and most of them are branched. The viral genome is a single strand of negative strand RNA, approximately 19 kb in length. The virus replicates, assembles, and is released in a budded manner in the cytoplasm of infected cells. However, few people know how EBOV invades the host pathway during infection. There is currently no specific treatment for Ebola virus disease. Due to its high infectivity and lethality, the development of new drugs for Ebola virus is a major Important issues are also a problem.
In the new study, the team generated an EBOV-host protein-protein interaction (PPI) map using affinity-labeled purification mass spectrometry (AP-MS) to attempt to clarify the relationship between human proteins and Ebola proteins. interaction. Not only did they discover the interaction between the Ebola virus transcriptional regulator VP30 and the human protein RBBP6, but also the 23 amino acid regions of RBBP6 binding to VP30 were identified by domain mapping. Further studies have shown that inhibition of endogenous RBBP6 stimulates viral transcription and increases Ebola virus replication; while stimulation of RBBP6 expression effectively inhibits Ebola virus transcription and replication, thereby preventing the virus from infecting the body. The role.
Through this breakthrough study, the research team demonstrated the potential of the biologics targeting VP30 binding interface to EB30 to treat Ebola virus, and suggested that RBBP6-derived peptides can effectively inhibit Ebola virus infection. Providing a new therapeutic strategy provides a powerful basis.
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