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基因突变是病毒进化的基础。新冠病毒为了更加适应人体宿主大环境,逃避免疫应答,可能会向着有利于其生存的方向进化,科研人员推测新冠病毒正以每月1-2个突变速率积累核苷酸变异。
7月,我国科学家在《Cell》发文,对新冠病毒变异进行系统性研究和介绍,从已知的刺突蛋白基因序列上鉴定出106个变异位点。《Science》也有相关的报道,称12月病毒毒株至少存在200个位点上的不同,与“初代”新冠病毒相比。目前,义翘神州已经成功开发超过70个突变体重组蛋白。
3月,D614G突变株成为欧洲的主要流行株,使病毒的感染率提高2.4-7.7倍。此后,多数突变株是在此基础上进行变异的,比如丹麦水貂突变Y453F,以及近期出现的英国突变N501Y和南非突变株。义翘神州也在最短的时间内,成功表达这些突变株的主要突变位点重组蛋白,支持科研人员进行突变株对新冠病毒传播、临床、诊断、疫苗及药物开发影响的研究。
新冠病毒Spike突变体蛋白
新冠病毒科研试剂库
在新冠疫情面前,义翘神州凭借坚实的技术基础和不断进取的创新精神,成功构建全球冠状病毒科研试剂库。义翘神州已经实现数百克级别的新冠试剂生产,并已成功生产重组蛋白、抗体、中和抗体、抗原检测试剂盒、芯片等相关新冠病毒试剂,用于科研、药物研发等领域。
新冠病毒科研试剂助力文献(选取部分)
义翘神州的新冠病毒科研试剂已经用于全球53个国家或地区的1700多家单位开展病毒研究、药物和疫苗开发,支持客户在Cell、Nature、Science等国际期刊发表文章超过200篇。
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1. Y Cao, et al. Potent Neutralizing Antibodies against SARS-CoV-2 Identified by High-Throughput Single-Cell Sequencing of Convalescent Patients’ B Cells. 9 July 2020, Cell.
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2. L Yurkovetskiy, et al. Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein Variant. 29 October 2020, Cell.
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3. D Wrapp, et al. Structural Basis for Potent Neutralization of Betacoronaviruses by Single-Domain Camelid Antibodies. 11 July 2020, Cell.
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4. Q Li, et al. The Impact of Mutations in SARS-CoV-2 Spike on Viral Infectivity and Antigenicity. 3 September 2020, Cell.
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5. L Liu, et al. Potent neutralizing antibodies against multiple epitopes on SARS-CoV-2 spike. 22 July 2020, Nature.
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6. KS Corbett, et al. SARS-CoV-2 mRNA vaccine design enabled by prototype pathogen preparedness. 5 August 2020, Nature.
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7. Z Ke, et al. Structures and distributions of SARS-CoV-2 spike proteins on intact virions. 17 August 2020, Nature.
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8. L Bao, et al. The pathogenicity of SARS-CoV-2 in hACE2 transgenic mice. 7 May 2020, Nature.
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9. X Chi, et al. A neutralizing human antibody binds to the N-terminal domain of the Spike protein of SARS-CoV-2. 7 August 2020, Science.
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10. B Rockx, et al. Comparative pathogenesis of COVID-19, MERS, and SARS in a nonhuman primate model. 29 May 2020, Science.
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11. JL Daly, et al. Neuropilin-1 is a host factor for SARS-CoV-2 infection. 13 November 2020, Science.
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12. R Yan, et al. Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2. 27 March 2020, Science.

