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Cellular & Molecular Immunology 2020年第6期17卷 613-620页

作者： Wanbo Tai Lei He Xiujuan Zhang Jing Pu Denis Voronin Shibo Jiang Yusen Zhou Lanying Du Lindsley F.Kimball Research Institute New York Blood CenterNew YorkNYUSA Beijing Institute of Microbiology and Epidemiology BeijingChina Key Laboratory of Medical Molecular Virology(MOE/NHC/CAMS) School of Basic Medical SciencesFudan UniversityShanghaiChina

The outbreak of Coronavirus Disease 2019(COVID-19)has posed a serious threat to global public health,calling for the development of safe and effective prophylactics and therapeutics against infection of its causative agent,severe acute respiratory syndrome coronavirus 2(SARS-CoV-2),also known as 2019 novel coronavirus(2019-nCoV).The CoV spike(S)protein plays the most important roles in viral attachment,fusion and entry,and serves as a target for development of antibodies,entry inhibitors and ***,we identified the receptor-binding domain(RBD)in SARS-CoV-2 S protein and found that the RBD protein bound strongly to human and bat angiotensin-converting enzyme 2(ACE2)***-CoV-2 RBD exhibited significantly higher binding affinity to ACE2 receptor than SARS-CoV RBD and could block the binding and,hence,attachment of SARS-CoV-2 RBD and SARS-CoV RBD to ACE2-expressing cells,thus inhibiting their infection to host ***-CoV RBD-specific antibodies could crossreact with SARS-CoV-2 RBD protein,and SARS-CoV RBD-induced antisera could cross-neutralize SARS-CoV-2,suggesting the potential to develop SARS-CoV RBD-based vaccines for prevention of SARS-CoV-2 and SARS-CoV infection.

关键词： 2019 novel coronavirus SARS-CoV-2 spike protein receptor-binding domain viral inhibitor cross-neutralization

An ultrapotent pan-β-coronavirus lineage B(β-CoV-B)neutralizing antibody locks the receptor-binding domain in closed conformation by targeting its conserved epitope

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Protein & Cell 2022年第9期13卷 655-675页

作者： Zezhong Liu Wei Xu Zhenguo Chen Wangjun Fu Wuqiang Zhan Yidan Gao Jie Zhou Yunjiao Zhou Jianbo Wu Qian Wang Xiang Zhang Aihua Hao Wei Wu Qianqian Zhang Yaming Li Kaiyue Fan Ruihong Chen Qiaochu Jiang Christian TMayer Till Schoofs Youhua Xie Shibo Jiang Yumei Wen Zhenghong Yuan Kang Wang Lu Lu Lei Sun Qiao Wang Key Laboratory of Medical Molecular Virology(MOE/NHC/CAMS) School of Basic Medical SciencesShanghai Institute of Infectious Disease and Biosecuritythe Fifth People’s Hospital of ShanghaiShanghai Key Laboratory of Medical EpigeneticsInternational Co-laboratory of Medical Epigenetics and Metabolism(Ministry of Science and Technology)Institutes of Biomedical SciencesBiosafety Level 3 LaboratoryShanghai Medical CollegeFudan UniversityShanghai 200032China CAS Key Laboratory of Infection and Immunity National Laboratory of MacromoleculesInstitute of BiophysicsChinese Academy of SciencesBeijing 100101China Experimental Immunology Branch Center for Cancer ResearchNational Cancer InstituteNational Institutes of HealthBethesdaMD 20892USA GSK Vaccines 1300 WavreBelgium

New threats posed by the emerging circulating variants of SARS-CoV-2 highlight the need to find conserved neutralizing epitopes for therapeutic antibodies and efficient vaccine ***,we identified a receptorbinding domain(RBD)-binding antibody,XG014,which potently neutralizesβ-coronavirus lineage B(β-CoV-B),including SARS-CoV-2,its circulating variants,SARSCoV and bat SARSr-CoV ***,antibody family members competing with XG014 binding show reduced levels of cross-reactivity and induce antibodydependent SARS-CoV-2 spike(S)protein-mediated cellcell fusion,suggesting a unique mode of recognition by *** analyses reveal that XG014 recognizes a conserved epitope outside the ACE2 binding site and completely locks RBD in the non-functional“down”conformation,while its family member XG005 directly competes with ACE2 binding and position the RBD“up”.Single administration of XG014 is effective in protection against and therapy of SARS-CoV-2 infection in *** findings suggest the potential to develop XG014 as pan-β-CoV-B therapeutics and the importance of the XG014 conserved antigenic epitope for designing broadly protective vaccines againstβ-CoV-B and newly emerging SARS-CoV-2 variants of concern.

关键词： SARS-CoV-2 neutralizing antibody receptor-binding domain XG014 antibody-dependent cellcell fusion

receptor-binding domain of SARS-Cov spike protein: Soluble expression in ***, purification and functional characterization

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World Journal of Gastroenterology 2005年第39期11卷 6159-6164页

作者： Jing Chen Lin Miao Jia-Ming Li Yan-Ying Li Qing-Yu Zhu Chang-Lin Zhou Hong-Qing Fang Hui-Peng Chen Institute of Biotechnology Academy of Military Medical Science Beijing 100071 China The Pharmaceutical University of China Nanjing 210009 Jiangsu Province China Institute of Microbiology and Epidemiology Academy of Military Medical Sciences Beijing 100071 China

AIM： To find a soluble and functional recombinant receptor-binding domain of severe acute respiratory syndrome-associated coronavirus （SARS-Cov）, and to analyze its receptor binding ability. METHODS： Three fusion tags （glutathione S-transferase, GST; thioredoxin, Trx; maltose-binding protein, MBP）, which preferably contributes to increasing solubility and to facilitating the proper folding of heteroprotein, were used to acquire the soluble and functional expression of RBD protein in Escherichia coli （BL21（DE3） and Rosetta-gamiB （DE3） strains）. The receptor binding ability of the purified soluble RBD protein was then detected by ELISA and flow cytometry assay. RESULTS： RBD of SARS-Cov spike protein was expressed as inclusion body when fused as TrxA tag form in both BL21 （DE3） and Rosetta-gamiB （DE3） under many different cultures and induction conditions. And there was no visible expression band on SDS-PAGE when RBD was expressed as MBP tagged form. Only GST tagged RBD was soluble expressed in BL21（DE3）, and the protein was purified by AKTA Prime Chromatography system. The ELISA data showed that *** antigen had positive reaction with anti-RBD mouse monoclonal antibody 1A5. Further flow cytometry assay demonstrated the high efficiency of RBD＇s binding ability to ACE2 （angiotensin-converting enzyme 2） positive Vero E6 cell. And ACE2 was proved as a cellular receptor that meditated an initial-affinity interaction with SARS-Cov spike protein. The geometrical mean of GST and *** binding to Vero E6 cells were 77.08 and 352.73 respectively. CONCLUSION： In this paper, we get sufficient soluble N terminal GST tagged RBD protein expressed in EcoliBL21 （DE3）; data from ELISA and flow cytometry assay demonstrate that the recombinant protein is functional and binding to ACE2 positive Vero E6 cell efficiently. And the recombinant RBD derived from *** can be used to developing subunit vaccine to block S protein binding with receptor and to neutralizing SARS-Cov infection.

关键词： receptor-binding domain SARS-Cov Spike protein expression E.coli

Identification of an ideal adjuvant for receptor-binding domain-based subunit vaccines against Middle East respiratory syndrome coronavirus

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Cellular & Molecular Immunology 2016年第2期13卷 180-190页

作者： Naru Zhang Rudragouda Channappanavar Cuiqing Ma Lili Wang Jian Tang Tania Garron Xinrong Tao Sumaiya Tasneem Lu Lu Chien-Te K Tseng Yusen Zhou Stanley Perlman Shibo Jiang Lanying Du Lindsley F. Kimball Research Institute New York Blood Center New York NY USA Department of Microbiology University of Iowa Iowa City IA USA State Key Laboratory of Pathogen and Biosecurity Beijing Institute of Microbiology and Epidemiology Beijing China Department of Microbiology and Immunology and Center for Biodefense and Emerging Disease University of Texas Medical Branch Galveston TX USA Key Laboratory of Medical Molecular Virology of Ministries of Education and Health Shanghai Medical College and Institute of Medical Microbiology Fudan University Shanghai China Xiang-Ya Medical College Central South University Changsha. China

Middle East respiratory syndrome （MERS）, an emerging infectious disease caused by MERS coronavirus （MERS-CoV）, has garnered worldwide attention as a consequence of its continuous spread and pandemic potential, making the development of effective vaccines a high priority. We previously demonstrated that residues 377-588 of MERS-CoV spike （S） protein receptor-binding domain （RBD） is a very promising MERS subunit vaccine candidate, capable of inducing potent neutralization antibody responses. In this study, we sought to identify an adjuvant that optimally enhanced the immunogenicity of S377-588 protein fused with Fc of human IgG （S377-588-Fc）. Specifically, we compared several commercially available adjuvants, including Freund＇s adjuvant, aluminum, Monophosphoryl lipid A, Montanide ISA51 and MF59 with regard to their capacity to enhance the immunogenicity of this subunit vaccine. In the absence of adjuvant, S377-588-Fc alone induced readily detectable neutralizing antibody and T-cell responses in immunized mice. However, incorporating an adjuvant improved its immunogenicity. Particularly, among the aforementioned adjuvants evaluated, MF59 is the most potent as judged by its superior ability to induce the highest titers of IgG, IgG1 and IgG2a subtypes, and neutralizing antibodies. The addition of MF59 significantly augmented the immunogenicity of S377-588-Fcto induce strong IgG and neutralizing antibody responses as well as protection against MERS-CoV infection in mice, suggesting that MF59 is an optimal adjuvant for MERS-CoV RBD-based subunit vaccines.

关键词： adjuvant effects MERS MERS-CoV receptor-binding domain subunit vaccine

Characterization of the receptor-binding domain of Ebola Glycoprotein in Viral Entry

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Virologica Sinica 2011年第3期26卷 156-170页

作者： JizhenWang BalajiManicassamy MichaelCaffrey LijunRong Department of Microbiology and Immunology College of Medicine University of Illinois at Chicago．Chicago．1L 60612．USA Department of Biochemistry and Molecular Genetics College of Medicine University of IllinoisatChicago Chicago IL 60607USA Current address for B．M：Department of Microbiology Mount Sinai School of Medicine l Gustave L． Levy Place Box 1124 New York．NY l0029 USA

Ebola virus infection causes severe hemorrhagic fever in human and non-human primates with high mortality. Viral entry/infection is initiated by binding of glycoprotein GP protein on Ebola virion to host cells, followed by fusion of virus-cell membrane also mediated by GP. Using an human immunodeficiency virus (HIV)-based pseudotyping system, the roles of 41 Ebola GP1 residues in the receptor-binding domain in viral entry were studied by alanine scanning substitutions. We identified that four residues appear to be involved in protein folding/structure and four residues are important for viral entry. An improved entry interference assay was developed and used to study the role of these residues that are important for viral entry. It was found that R64 and K95 are involved in receptor binding. In contrast, some residues such as I170 are important for viral entry, but do not play a major role in receptor binding as indicated by entry interference assay and/or protein binding data, suggesting that these residues are involved in post-binding steps of viral entry. Furthermore, our results also suggested that Ebola and Marburg viruses share a common cellular molecule for entry.

关键词： receptor-binding domain Ebola virus Glycoprotein Viral Entry

Understanding neutralising antibodies against SARS-CoV-2 and theirimplications in clinical practice

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Military Medical Research 2022年第2期9卷 215-230页

作者： Natalie Yan-Lin Pang Alexander Shao-Rong Pang Vincent T.Chow De-Yun Wang Yong Loo Lin School of Medicine National University of SingaporeSingapore 119228Singapore Department of Microbiology and Immunology National University of SingaporeScience Drive 2Singapore 117545Singapore Infectious Diseases Translational Research Program Yong Loo Lin School of MedicineNational University of SingaporeSingapore 119228Singapore Department of Otolaryngology Yong Loo Lin School of MedicineNational University of Singapore1E Kent Ridge RoadSingapore 119228Singapore

Severe acute respiratory syndrome coronavirus (SARS-CoV-2) is a newly identified member of the coronavirus family that has caused the coronavirus disease 2019 (COVID-19) pandemic. This rapidly evolving and unrelenting SARS-CoV-2has disrupted the lives and livelihoods of millions worldwide. As of 23 August 2021, a total of 211,373,303 COVID-19cases have been confirmed globally with a death toll of 4,424,341. A strong understanding of the infection pathway of SARS-CoV-2, and how our immune system responds to the virus is highly pertinent for guiding the development and improvement of effective treatments. In this review, we discuss the current understanding of neutralising antibodies(NAbs) and their implications in clinical practice. The aspects include the pathophysiology of the immune response,particularly humoral adaptive immunity and the roles of NAbs from B cells in infection clearance. We summarise the onset and persistence of IgA, IgM and IgG antibodies, and we explore their roles in neutralising SARS-CoV-2, their persistence in convalescent individuals, and in reinfection. Furthermore, we also review the applications of neutralising antibodies in the clinical setting—from predictors of disease severity to serological testing to vaccinations, and finally in therapeutics such as convalescent plasma infusion.

关键词： Severe acute respiratory syndrome coronavirus Coronavirus disease 2019 Neutralising antibodies Persistence Spike glycoprotein receptor-binding domain B cells T cells Convalescent plasma

Evidence for a mouse origin of the SARS-CoV-2 Omicron variant

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Journal of Genetics and Genomics 2021年第12期48卷 1111-1121页

作者： Changshuo Wei Ke-Jia Shan Weiguang Wang Shuya Zhang Qing Huan Wenfeng Qian State Key Laboratory of Plant Genomics Institute of Genetics and Developmental BiologyInnovation Academy for Seed DesignChinese Academy of SciencesBeijing 100101China University of Chinese Academy of Sciences Beijing 100049China

The rapid accumulation of mutations in the SARS-CoV-2 Omicron variant that enabled its outbreak raises questions as to whether its proximal origin occurred in humans or another mammalian host. Here, we identified 45 point mutations that Omicron acquired since divergence from the B.1.1 lineage. We found that the Omicron spike protein sequence was subjected to stronger positive selection than that of any reported SARS-CoV-2 variants known to evolve persistently in human hosts, suggesting a possibility of hostjumping. The molecular spectrum of mutations(i.e., the relative frequency of the 12 types of base substitutions) acquired by the progenitor of Omicron was significantly different from the spectrum for viruses that evolved in human patients but resembled the spectra associated with virus evolution in a mouse cellular environment. Furthermore, mutations in the Omicron spike protein significantly overlapped with SARS-CoV-2 mutations known to promote adaptation to mouse hosts, particularly through enhanced spike protein binding affinity for the mouse cell entry receptor. Collectively, our results suggest that the progenitor of Omicron jumped from humans to mice, rapidly accumulated mutations conducive to infecting that host,then jumped back into humans, indicating an inter-species evolutionary trajectory for the Omicron outbreak.

关键词： SARS-CoV-2 Omicron Evolutionary origins Molecular spectrum of mutations Spike-ACE2 interaction receptor-binding domain