還記得炒的沸沸揚揚的武漢新冠病毒上一個新Furin酶切點嗎？現在有人把它拿掉了，病毒的毒性大部消失了！

大家都還記得炒的沸沸揚揚的武漢新冠病毒上一個新Furin酶切點嗎？現在有人把它拿掉了，病毒的毒性大部消失了！失去在肺上皮細胞繁殖的功能，但在其他細胞中，還可以繼續繁殖。這是一篇最新的已審閱的priprint報道，是來自美國多家實驗室合作研究的結果：

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7457603/pdf/nihpp-2020.08.26.268854.pdf

https://pubmed.ncbi.nlm.nih.gov/32869021/

作者中不乏中國同胞，結論和載要如下：

Furin Cleavage Site Is Key to SARS-CoV-2 Pathogenesis

Bryan A Johnson, Xuping Xie, Birte Kalveram, Kumari G Lokugamage, Antonio Muruato, Jing Zou, Xianwen Zhang, Terry Juelich, Jennifer K Smith, Lihong Zhang, Nathen Bopp, Craig Schindewolf, Michelle Vu, Abigail Vanderheiden, Daniele Swetnam, Jessica A Plante, Patricia Aguilar, Kenneth S Plante, Benhur Lee, Scott C Weaver, Mehul S Suthar, Andrew L Routh, Ping Ren, Zhiqiang Ku, Zhiqiang An, Kari Debbink, Pei Yong Shi, Alexander N Freiberg, Vineet D Menachery

 

• PMID: 32869021
•  
• PMCID: PMC7457603
•  
• DOI: 10.1101/2020.08.26.268854

Free PMC article

Abstract

SARS-CoV-2 has resulted in a global pandemic and shutdown economies around the world. Sequence analysis indicates that the novel coronavirus (CoV) has an insertion of a furin cleavage site (PRRAR) in its spike protein. Absent in other group 2B CoVs, the insertion may be a key factor in the replication and virulence of SARS-CoV-2. To explore this question, we generated a SARS-CoV-2 mutant lacking the furin cleavage site (ΔPRRA) in the spike protein. This mutant virus replicated with faster kinetics and improved fitness in Vero E6 cells. The mutant virus also had reduced spike protein processing as compared to wild-type SARS-CoV-2. In contrast, the ΔPRRA had reduced replication in Calu3 cells, a human respiratory cell line, and had attenuated disease in a hamster pathogenesis model. Despite the reduced disease, the ΔPRRA mutant offered robust protection from SARS-CoV-2 rechallenge. Importantly, plaque reduction neutralization tests (PRNT 50 ) with COVID-19 patient sera and monoclonal antibodies against the receptor-binding domain found a shift, with the mutant virus resulting in consistently reduced PRNT 50 titers. Together, these results demonstrate a critical role for the furin cleavage site insertion in SARS-CoV-2 replication and pathogenesis. In addition, these findings illustrate the importance of this insertion in evaluating neutralization and other downstream SARS-CoV-2 assays.