检索结果-南通市图书馆

Sequence difference of angiotensin-converting enzyme 2 between nonhuman primates affects its binding-affinity with SARS-CoV-2 S receptor binding domain

引用

Biosafety and Health 2022年第5期4卷 293-298页

作者： Xiaojun Zhou Jingjing Zhao Yefeng Qiu Rui Jia Department of Biosafety China Biotechnology Co.LTDBeijing 100025China Department of Infectious Diseases Beijing Chaoyang HospitalCapital Medical UniversityBeijing 100043China Laboratory Animal Center Academy of Military Medical SciencesBeijing 100071China

Severe acute respiratory syndrome coronavirus 2(SARS-CoV-2)has caused many deaths and contributed to a tremendous public health concern worldwide since ***-converting enzyme 2(ACE2)binds to the SARS-CoV-2 virus as a *** challenge of different nonhuman primate(NHP)species by SARSCoV-2 virus demonstrated different effects on virus replication and disease *** study characterizes differences between host ACE2 sequences of three NHP species:Macaca mulatta,Macaca fascicularis,and Chlorocebus *** addition,the binding affinity between the ACE2 ectodomain and the SARS-CoV-2 S receptor-binding domain(RBD)was *** of ACE2 sequence among NHP species and the binding affinity may account for different susceptibility and responses to SARS-CoV-2 infection.

关键词： SARS-CoV-2 Angiotensin-converting enzyme 2 receptor binding domain Surface plasmon resonance African green monkey

来源：

维普期刊数据库

同方期刊数据库评论

在线全文

学校读者我要写书评

暂无评论

The S190R mutation in the hemagglutinin protein of pandemic H1N1 2009 influenza virus increased its pathogenicity in mice

引用

Science China(Life Sciences) 2018年第7期61卷 836-843页

作者： Yongkun Chen Tian Bai Wenfei Zhu Rongbao Gao Zhihong Deng Yi Shi Shumei Zou Yiwei Huang Xiyan Li Fangcai Li Zhaomin Feng Tao Chen Jing Yang Dayan Wang Lidong Gao Yuelong Shu National Institute for Viral Disease Control and Prevention Collaboration Innovation Center for Diagnosis and Treatment of Infectious DiseasesChinese Center for Disease Control and PreventionKey Laboratory for Medical VirologyNational Health and Family Planning CommissionBeijing 102206China Hunan Provincial Center for Disease Control and Prevention Changsha 410005China CAS Key Laboratory of Pathogenic Microbiology and Immunology Institute of MicrobiologyChinese Academy of SciencesBeijing 100101 China School of Public Health(Shenzhen) Sun Yat-sen UniversityGuangzbou 510275China

Human influenza viruses preferentially bind to sialic acid-α2,6-galactose (SAα2,6Gal) receptors, which are predominant in human upper respiratory epithelia, whereas avian influenza viruses preferentially bind to SAα2,3Gal receptors. However, variants with amino acid substitutions around the receptor-binding sites of the hemagglutinin (HA) protein can be selected after several passages of human influenza viruses from patients’ respiratory samples in the allantoic cavities of embryonated chicken eggs. In this study, we detected an egg-adapted HA S190R mutation in the pandemic H1N1 virus 2009 (pdmH1N1), and evaluated the effects of this mutation on receptor binding affinity and pathogenicity in mice. Our results revealed that residue 190 is located within the pocket structure of the receptor binding site. The single mutation to arginine at position 190 slightly increased the binding affinity of the virus to the avian receptor and decreased its binding to the long human α2,6-linked sialic acid receptor. Our study demonstrated that the S190R mutation resulted in earlier death and higher weight loss in mice compared with the wild-type virus. Higher viral titers at 1 dpi (days post infection) and diffuse damage at 4 dpi were observed in the lung tissues of mice infected with the mutant virus.

关键词： pandemic HIN1 2009 influenza virus egg adaptation HA mutation receptor binding domain pathogenicity mice

来源：

维普期刊数据库

同方期刊数据库评论

在线全文

学校读者我要写书评

暂无评论

Prediction of Proteins Associated with COVID-19 Based Ligand Designing and Molecular Modeling

引用

Computer Modeling in Engineering & Sciences 2020年第12期125卷 907-926页

作者： Majid Monajjemi Rahim Esmkhani Fatemeh Mollaamin Sara Shahriari Department of Chemical Engineering Central Tehran BranchIslamic Azad UniversityTehran14987-54891Iran Department of Chemistry Khoy BranchIslamic Azad UniversityKhoy58159-88838Iran Department of Chemistry Central Tehran BranchIslamic Azad UniversityTehran***Iran

Current understanding about how the virus that causes COVID-19 spreads is largely based on what is known about similar *** of the Natural products are suitable drugs against SARS-CoV-2 main *** recognizing a strong inhibitor,we have accomplished dock-ing studies on the major virus protease with 4 natural product species as anti COVID-19(SARS-CoV-2),namely“Vidarabine”,“Cytarabine”,“Gem-citabine”and“Matrine”which have been extracted fromGillan’s leaves *** are known as Chuchaq,Trshvash,Cote-Couto and Khlvash in *** these four studied compounds,Cytarabine appears as a suitable com-pound with high effectiveness inhibitors to this *** by this work we present a method on the Computational Prediction of Protein Structure Associated with COVID-19 Based Ligand Design and Molecular *** this investigation,auto dock software(iGEM-DOCK)has been used and via this tool,the suitable receptors can be distinguished in whole COVID-19 component structures for forming a complex.“iGEMDOCK”is suitable to define the binding site *** docking simulation and NMR inves-tigation,we have demonstrated these compounds exhibit a suitable binding energy around 9 Kcal/mol with various ligand proteins modes in the bind-ing to COVID-19 ***,these data need further evaluation for repurposing these drugs against COVID-19 viruses,in both vivo&vitro.

关键词： COVID-19 receptor binding domain Gillan’s leaves plants angiotensin converting enzyme-2 protease domain

来源：

维普期刊数据库评论

在线全文

维普期刊数据库

学校读者我要写书评

暂无评论

Molecular dynamics-driven exploration of peptides targeting SARS-CoV-2,with special attention on ACE2,S protein,M^(pro),and PL^(pro):A review

引用

BIOCELL 2023年第8期47卷 1727-1742页

作者： MOHAMAD ZULKEFLEE SABRI JOANNA BOJARSKA FAI-CHU WONG TSUN-THAI CHAI Green Chemistry and Sustainable Technology Cluster Bioengineering SectionUniversiti Kuala LumpurMalaysian Institute of Chemical and Bioengineering Technology(UniKL MICET)Alor Gajah78000Malaysia Institute of General and Ecological Chemistry Faculty of ChemistryLodz University of TechnologyLodz90-924Poland Department of Chemical Science Faculty of ScienceUniversiti Tunku Abdul RahmanKampar31900Malaysia Center for Agriculture and Food Research Universiti Tunku Abdul RahmanKampar31900Malaysia

Molecular dynamics(MD)simulation is a computational technique that analyzes the movement of a system of particles over a given *** can provide detailed information about the fluctuations and conformational changes of biomolecules at the atomic level over *** recent years,MD has been widely applied to the discovery of peptides and peptide-like molecules that may serve as severe acute respiratory syndrome coronavirus 2(SARS-CoV-2)*** review summarizes recent advances in such explorations,focusing on four protein targets:angiotensin-converting enzyme 2(ACE2),spike protein(S protein),main protease(M^(pro)),and papain-like protease(PL^(pro)).These four proteins are important druggable targets of SARS-CoV-2 because of their roles in viral entry,maturation,and infectivity of the virus.A review of the literature revealed that ACE2,S protein,and M^(pro) have received more attention in MD research than PL^(pro).Inhibitors of the four targets identified by MD simulations included peptides derived from food and other bioresources,peptides designed using the targets as templates,and peptide-like molecules retrieved from *** of the inhibitors have yet to be validated in experimental assays for ***,the role of MD simulation as an efficient tool in the early stages of anti-SARS-CoV-2 drug discovery agents has been demonstrated.

关键词： COVID-19 Anti-SARS-CoV-2 agent receptor binding domain Computational screening Drug discovery

来源：

维普期刊数据库评论

在线全文

维普期刊数据库

学校读者我要写书评

暂无评论

Inactivating SARS-CoV-2 by electrochemical oxidation

引用

Science Bulletin 2021年第7期66卷 720-726,M0004页

作者： Yunchuan Tu Wei Tang Liang Yu Zheyi Liu Yanting Liu Huicong Xia Haiwei Zhang Shiyun Chen Jia Wu Xiaoju Cui Jianan Zhang Fangjun Wang Yangbo Hu Dehui Deng State Key Laboratory of Catalysis Collaborative Innovation Center of Chemistry for Energy MaterialsDalian Institute of Chemical PhysicsChinese Academy of SciencesDalian 116023China Key Laboratory of Special Pathogens and Biosafety Wuhan Institute of VirologyCenter for Biosafety Mega-ScienceChinese Academy of SciencesWuhan 430071China CAS Key Laboratory of Separation Sciences for Analytical Chemistry Dalian Institute of Chemical PhysicsChinese Academy of SciencesDalian 116023China University of Chinese Academy of Sciences Beijing 100049China College of Materials Science and Engineering Zhengzhou UniversityZhengzhou 450001China Wuhan Institute of Virology Center for Biosafety Mega-ScienceChinese Academy of SciencesWuhan 430071China

Fully inactivating SARS-Co V-2, the virus causing coronavirus disease 2019, is of key importance for interrupting virus transmission but is currently performed by using biologically or environmentally hazardous disinfectants. Herein, we report an eco-friendly and efficient electrochemical strategy for inactivating the SARS-Co V-2 using in-situ formed nickel oxide hydroxide as anode catalyst and sodium carbonate as electrolyte. At a voltage of 5 V, the SARS-Co V-2 viruses can be rapidly inactivated with disinfection efficiency reaching 95% in only 30 s and 99.99% in 5 min. Mass spectrometry analysis and theoretical calculations indicate that the reactive oxygen species generated on the anode can oxidize the peptide chains and induce cleavage of the peptide backbone of the receptor binding domain of the SARS-Co V-2 spike glycoprotein, and thereby disables the virus. This strategy provides a sustainable and highly efficient approach for the disinfection of the SARS-CoV-2 viruliferous aerosols and wastewater.

关键词： Electrochemical oxidation Reactive oxygen specie receptor binding domain SARS-Co V-2

来源：

维普期刊数据库

同方期刊数据库评论

在线全文

学校读者我要写书评

暂无评论

欢迎您,

建议与咨询留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

时间限定

文献类型

馆藏选择

核心期刊

语言

文献类型

帮助

文字说明：

检索规则说明：

检索范例：

分类表

所选分类

限定检索结果

文献类型

馆藏范围

日期分布

学科分类号

主题

机构

作者

语言

在线全文

在线全文

在线全文

在线全文

在线全文

请选择保存的检索档案：

请选择收藏分类：

通借通还

欢迎您,

建议与咨询 留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

时间限定

文献类型

馆藏选择

核心期刊

语言

文献类型

帮助

文字说明：

检索规则说明：

检索范例：

分类表

所选分类

限定检索结果

文献类型

馆藏范围

日期分布

学科分类号

主题

机构

作者

语言

在线全文

在线全文

在线全文

在线全文

在线全文

请选择保存的检索档案： 新增检索档案 确定 取消

请选择收藏分类： 新增自定义分类 确定 取消

通借通还

建议与咨询留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

请选择保存的检索档案：

请选择收藏分类：