10 results on '"Liu, Yunchao"'
Search Results
2. Precise location of two novel linear epitopes on the receptor-binding domain surface of MERS-CoV spike protein recognized by two different monoclonal antibodies.
- Author
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Wang P, Ding P, Wei Q, Liu H, Liu Y, Li Q, Xing Y, Li G, Zhou E, and Zhang G
- Subjects
- Animals, Antibodies, Monoclonal, Murine-Derived genetics, Antibodies, Viral genetics, Epitopes genetics, HEK293 Cells, Humans, Mice, Mice, Inbred BALB C, Middle East Respiratory Syndrome Coronavirus genetics, Protein Domains, Sf9 Cells, Spike Glycoprotein, Coronavirus genetics, Spodoptera, Antibodies, Monoclonal, Murine-Derived immunology, Antibodies, Viral immunology, Epitope Mapping, Epitopes immunology, Middle East Respiratory Syndrome Coronavirus immunology, Spike Glycoprotein, Coronavirus immunology
- Abstract
Middle East respiratory syndrome coronavirus (MERS-CoV) is a coronavirus which can cause severe human respiratory diseases with a fatality rate of almost 36%. In this study, we report the generation, characterization and epitope mapping of several monoclonal antibodies against the spike receptor-binding domain (RBD) of MERS-CoV. Two monoclonal antibodies (4C7 and 6E8) that can react with linearized RBD have been selected for subsequent identification of RBD mAb-binding epitopes. Two distinct novel linear epitopes,
423 FTCSQIS429 and546 SPLEGGGWL554 ,were precisely located at the outermost surface of RBD by dot-blot hybridization and ELISAs. Multiple sequence alignment analysis showed that these two peptides were highly conserved. Alanine (A)-scanning mutagenesis demonstrated that residues 423F, 428I, and 429S are the crucial residues for the linear epitope423 FTCSQIS429 while residues 548L, 550G, 553W, 554L for epitope546 SPLEGGGWL554 . These findings may be helpful for further understanding of the function of RBD protein and the development of subsequent diagnosis and detection methods., (Copyright © 2021 Elsevier B.V. All rights reserved.)- Published
- 2022
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3. A novel linear epitope at the C-terminal region of the classical swine fever virus E2 protein elicits neutralizing activity.
- Author
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Xu Q, Guo J, Ma F, Liu L, Wang Y, Zhang S, Niu X, Li X, Jiang M, Wang Y, Wang L, Liu Y, Li Q, Chai S, Wang R, Ma Q, Zhang E, and Zhang G
- Subjects
- Amino Acid Sequence, Animals, Antibodies, Monoclonal immunology, Antibody Specificity immunology, Conserved Sequence, Female, Mice, Inbred BALB C, Models, Molecular, Peptide Library, Mice, Antibodies, Neutralizing immunology, Classical Swine Fever Virus chemistry, Classical Swine Fever Virus immunology, Epitopes immunology, Viral Envelope Proteins chemistry, Viral Envelope Proteins immunology
- Abstract
Classical swine fever virus (CSFV) is a member of the genus Pestivirus, which causes serious economic losses. The re-emergence of the disease in Japan in 2018 has increased awareness of CSFV. In this study, Balb/c mice were immunized with plant-derived E2 protein, and four monoclonal antibodies (mAbs) 4B11, 7B3, 11A5 and 6F3 were generated. Two of these mAbs, 4B11 and 7B3, effectively blocked CSFV infection of PK-15 cells. Both mAbs recognized a novel linear epitope,
256 CLIGNTTVKVHASDER271 . The neutralizing ability of anti-CSFV serum decreased 63%, when pre-incubated with the linear peptide at 200 μg/mL. Structural analysis showed that this linear epitope is present at the border of Domain C and Domain D on the surface of the E2 protein. Alignment of amino acid sequences showed that the epitope was conserved in different subgroups of CSFV but not in other members of the Pestivirus genus. Consistently with the analysis above, this epitope distinguished antibodies against CSFV from those against bovine viral diarrhea virus (BVDV). Our study provides an ideal candidate peptide for new vaccine design and differential diagnosis of CSFV. These findings will contribute to the control and eradication of classical swine fever., (Copyright © 2021 Elsevier B.V. All rights reserved.)- Published
- 2021
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4. A monoclonal antibody neutralizes pesudorabies virus by blocking gD binding to the receptor nectin-1.
- Author
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Zhang T, Liu Y, Chen Y, Wang J, Feng H, Wei Q, Zhao S, Yang S, Liu D, and Zhang G
- Subjects
- Animals, Antibodies, Monoclonal immunology, Antibodies, Monoclonal pharmacology, Antibodies, Neutralizing immunology, Antibodies, Neutralizing pharmacology, Antibodies, Viral pharmacology, Cell Line, Glycoproteins chemistry, Herpesvirus 1, Suid pathogenicity, Humans, Nectins antagonists & inhibitors, Nectins immunology, Nervous System Diseases immunology, Nervous System Diseases virology, Protein Binding drug effects, Protein Binding immunology, Pseudorabies genetics, Pseudorabies immunology, Pseudorabies virology, Swine virology, Viral Envelope Proteins chemistry, Viral Envelope Proteins genetics, Glycoproteins genetics, Herpesvirus 1, Suid drug effects, Nectins genetics, Nervous System Diseases prevention & control, Pseudorabies drug therapy
- Abstract
Pseudorabies virus (PRV) was isolated from some human cases recently and the infected patients manifested respiratory dysfunction and acute neurological symptoms. However, no effective drug or vaccine, preventing the progression of PRV infection, is available. Nectin-1 was the only reported receptor for PRV cell entry both swine and human origin, representing an excellent target to block PRV infection, and especially its transmission from pigs to humans. A PRV-gD specific mAbs (10B6) was isolated from hybridomas and its neutralizing activities in vitro and in vivo were determined. 10B6 exhibited effective neutralizing activities in vitro with IC
50 = 2.514 μg/ml and 4.297 μg/ml in the presence and absence of complement. And in vivo, 10B6 provided 100% protection against PRV lethal challenge with a dose of 15 mg/kg. Further, 10B6 could bind to a conserved epitope,316 QPAEPFP322 , locating in gD pro-fusion domain, and finally blocks the binding of PRV-gD to nectin-1. Moreover, 10B6 showed an effective inhibition on PRV cell-attachment in a cell type-independent manner and could also block the virus spreading among cells. 10B6 exhibited effectively neutralizing activities to Chinese PRV variant strain in vitro and in vivo by blocking gD binding to nectin-1, implied both prophylactic and therapeutic interventions against PRV infections., (Copyright © 2021 Elsevier B.V. All rights reserved.)- Published
- 2021
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5. Antiviral activity of porcine interferon delta 8 against pesudorabies virus in vitro.
- Author
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Zhang T, Liu Y, Chen Y, Wang J, Feng H, Wei Q, Zhao S, Yang S, Ma H, Liu D, and Zhang G
- Subjects
- Animals, Cell Line, Drosophila, Protective Agents pharmacology, Pseudorabies virology, Swine, Antiviral Agents pharmacology, Herpesvirus 1, Suid drug effects, Interferon Type I pharmacology, Pseudorabies drug therapy
- Abstract
Recently, pseudorabies virus (PRV) was isolated from human cases, and infected patients presented with respiratory dysfunction and acute neurological symptoms. However, there was no available effective drug to prevent the progression of PRV infection. In the present study, we screened a stably Drosophila S2 cell line which can secretory express a novel type I IFNs-interferon delta 8 (IFN-δ8) and the yield was about 10 mg/L. After purification, recombinant IFN-δ8 was demonstrated to be acid-stable, heat-stable, and nontoxic to PK-15 and 3D4/21 cells. Antiviral effects of IFN-δ8 against PRV were tested in vitro. Our results showed both pre- and post-treatment, recombinant PoIFN-δ8 exerted a significant protective effect against PRV infection in PK-15 and 3D4/21 cells. In addition, PoIFN-δ8 remarkably increased the expression of eight IFN-stimulated genes (ISGs), including ISG15, OAS1, PKR, MX1, CH25H, IFITM1, IFITM2 and IFITM3, to resist virus infection. These findings highlight the significance of IFN-δ8 that might serve as an antiviral agent for the prevention of PRV infection, and maybe expand the potential function of IFN antiviral drugs in the future., Competing Interests: Declaration of competing interest The authors declare that they have no competing interests., (Copyright © 2021 Elsevier B.V. All rights reserved.)
- Published
- 2021
- Full Text
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6. Reasonable permutation of M2e enhances the effect of universal influenza nanovaccine.
- Author
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Ding P, Zhang G, Chen Y, Liu H, Liu Y, Jia R, Wang Y, Li G, and Wang A
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- Animals, Birds, Capsid Proteins chemistry, Capsid Proteins immunology, Female, Humans, Immunization, Influenza Vaccines immunology, Mice, Nanoparticles, Protein Conformation, Protein Domains, Recombinant Fusion Proteins administration & dosage, Recombinant Fusion Proteins immunology, Swine, Vaccines, Combined administration & dosage, Vaccines, Combined immunology, Viral Matrix Proteins chemistry, Viral Matrix Proteins immunology, Capsid Proteins metabolism, Circovirus immunology, Influenza A virus immunology, Influenza Vaccines administration & dosage, Receptors, Antigen, B-Cell metabolism, Viral Matrix Proteins metabolism
- Abstract
Influenza A virus (IAV) occasionally cross-species transmission among humans, swine and avian. The ectodomain of matrix protein 2 (M2e) is highly conserved in IAV, and multi-copy M2e from different species are usually displayed on the surface of nanoparticles to improve immunogenicity and constitute universal IAV nanovaccines. In our previous study, three M2e were inserted into the C-terminal of Cap protein of porcine circovirus type 2 (PCV2) to form a universal nanovaccine that provides protection against PCV2 and different subtypes of IAV. However, M2e adopts at least two converted conformations, and the intermolecular linker of M2e enhances the conformational instability, which limits the recognition by B cell receptors and production of high-level antibodies. Here, we report that the permutation of M2e affects effectiveness of nanovaccines. Three M2e derived from humans, swine and avian IAV were inserted into the C-terminal of Cap protein to form nanovaccines. Immunoprotective effects of different M2e arrangements were explored in mice. Results showed that the M2e closest to the surface of nanoparticle induced the most efficient protection against IAV derived from corresponding species. The results will contribute to develop more effective PCV2 and universal IAV bivalent nanovaccines for pigs, as well as species-specific universal IAV vaccines., Competing Interests: Declaration of competing interest The authors report no conflicts of interest are associated with this work., (Copyright © 2021. Published by Elsevier B.V.)
- Published
- 2021
- Full Text
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7. Identification of a dominant linear epitope on the VP2 capsid protein of porcine parvovirus and characterization of two monoclonal antibodies with neutralizing abilities.
- Author
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Liu Y, Wang J, Chen Y, Wang A, Wei Q, Yang S, Feng H, Chai S, Liu D, and Zhang G
- Subjects
- Animals, Antibodies, Monoclonal immunology, Antibodies, Neutralizing genetics, Antibodies, Neutralizing immunology, Capsid Proteins immunology, Epitopes immunology, Parvovirus, Porcine immunology, Swine genetics, Swine virology, Antibodies, Monoclonal genetics, Capsid Proteins genetics, Epitopes genetics, Parvovirus, Porcine genetics
- Abstract
Porcine parvovirus (PPV) is a major cause of reproductive failure in swine, and has caused huge losses throughout the world. The structural viral protein VP2, which is able to self-assemble into empty capsids, known as virus-like particles (VLPs), is crucial to induce PPV-specific neutralizing antibodies and protective immunity. In this study, twelve monoclonal antibodies (mAbs) against PPV were generated. The mAbs were characterized by indirect enzyme-linked immunosorbent assay (ELISA), western blotting (WB) and virus neutralization (VN) assay. Two mAbs were defined to be able to neutralize the standard PPV 7909 strain. Subsequently, peptide scanning was applied to identify linear epitopes. The peptide,
89 ESGVAGQMV97 was defined as a precise linear epitope. Results from structural analysis showed that the epitope was exposed on the virion surface. Multiple sequence alignment analysis indicated that peptide89 ESGVAGQMV97 was not completely conserved, with a higher amino acid mutation rate at91 G,92 V and93 A position. Alanine-scanning mutagenesis further revealed that residues89 E,90 S,91 G,92 V and94 G were the core sites involved in antibody recognition. These findings may facilitate further understanding the function of the VP2 protein and development of diagnostic tools., Competing Interests: Declaration of competing interest The authors declare that they have no competing interests., (Copyright © 2020. Published by Elsevier B.V.)- Published
- 2020
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8. Soluble FMDV VP1 proteins fused with calreticulin expressed in Escherichia coli under the assist of trigger factor16 (Tf16) formed into high immunogenic polymers.
- Author
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Liu C, Feng H, Liu Y, Chen Y, Yang S, Deng R, and Zhang G
- Subjects
- Capsid Proteins chemistry, Cell Line, Cytokines metabolism, Gene Expression, Lymphocytes immunology, Lymphocytes metabolism, Recombinant Fusion Proteins chemistry, Solubility, Bacterial Proteins genetics, Calreticulin genetics, Capsid Proteins genetics, Capsid Proteins immunology, Escherichia coli genetics, Recombinant Fusion Proteins genetics, Recombinant Fusion Proteins immunology
- Abstract
Foot and mouth disease virus (FMDV) is a highly contagious pathogen propagating among cloven-hoofed animals. As a major immunogenic protein, VP1 plays a pivotal role in the induction of neutralizing antibodies, which therefore is an ideal target for developing subunit vaccines. In current study, four prokaryotic expression clones (rV4C, rC4V, rV5F and rF5V) were constructed by fusing truncated calreticulin (CRT) (120-250 aa or 120-308 aa) at the N/C terminal of vp1 gene, and co-expressed with chaperone trigger factor 16 (Tf16) in E.coli, respectively. The soluble recombinant CRT-fused VP1 proteins could form into homogeneous reactive polymers with average hydrodynamic diameters around 100 nm according to the dynamic light scattering (DLS) data. Immunization of guinea pigs with 10 μg purified CRT-fused VP1 proteins induced high levels of antibodies against naked-VP1 through indirect ELISA. Sandwich ELISA showed that only rC4V could elicit the same level of antibody against FMD virus as commercial inactivated vaccine after booster. The lymphocyte cytokines secretion of immunized rC4V was higher than the other CRT-fused VP1 proteins in guinea pigs. These results showed that the soluble CRT-fused VP1 proteins, especially rC4V, expressed with Tf16 in E. coli might have potential to be used as subunit vaccine candidate against FMDV., Competing Interests: Declaration of competing interest The authors declare that they have no competing interests., (Copyright © 2019 Elsevier B.V. All rights reserved.)
- Published
- 2020
- Full Text
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9. Unravelling the receptor binding property of egg drop syndrome virus (EDSV) from the crystal structure of EDSV fiber head.
- Author
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Song Y, Wei Q, Liu Y, Feng H, Chen Y, Wang Y, Bai Y, Xing G, Deng R, and Zhang G
- Subjects
- Adenoviridae Infections veterinary, Amino Acid Sequence, Animals, Cells, Cultured, Ducks, Gene Expression, Gene Knockdown Techniques, Humans, Optical Imaging, Protein Binding, Protein Interaction Domains and Motifs, Recombinant Proteins, Structure-Activity Relationship, Atadenovirus physiology, Capsid Proteins chemistry, Capsid Proteins metabolism, Models, Molecular, Protein Conformation, Receptors, Virus chemistry, Receptors, Virus metabolism
- Abstract
Egg drop syndrome virus (EDSV) is an avian adenovirus that causes markedly decrease in egg production, and in the quality of the eggs when it infects chickens. Until now, EDSV virus-cell interactions are poorly understood, and the cellular receptor is still unknown. In the present study, we determined the atomic structure of the fiber head of EDSV (residues 377-644) at 2.74 Å resolution. Structure comparison with the (chick embryo lethal orphan) CELO long fiber head and human adenovirus fiber heads reveals that the avian adenovirus may interact with the same attachment factor in a unique fashion. Based on the previous studies of CELO virus, we assumed that the chicken coxsackievirus and adenovirus receptor (CAR) may be the attachment factor. We then demonstrate that the chicken CAR serves as a cellular attachment factor for EDSV based on three lines of evidences. Taken together, the results presented here are helpful for further exploring the pathogenesis related to the interaction between EDSV and host cells, and may be used for vaccine development and intervention strategies against EDSV infection., (Copyright © 2019 Elsevier B.V. All rights reserved.)
- Published
- 2019
- Full Text
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10. Porcine parvovirus capsid protein expressed in Escherichia coli self-assembles into virus-like particles with high immunogenicity in mice and guinea pigs.
- Author
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Ji P, Liu Y, Chen Y, Wang A, Jiang D, Zhao B, Wang J, Chai S, Zhou E, and Zhang G
- Subjects
- Animals, Antibodies, Neutralizing blood, Antigens, Viral administration & dosage, Capsid Proteins administration & dosage, Cytokines metabolism, Escherichia coli genetics, Guinea Pigs, Hemagglutination Inhibition Tests, Lymphocyte Activation, Mice, Parvovirus, Porcine chemistry, Spleen virology, Swine, Vaccines, Subunit administration & dosage, Vaccines, Subunit genetics, Vaccines, Subunit immunology, Vaccines, Virus-Like Particle administration & dosage, Vaccines, Virus-Like Particle chemistry, Vaccines, Virus-Like Particle genetics, Antigens, Viral genetics, Antigens, Viral metabolism, Capsid Proteins genetics, Capsid Proteins metabolism, Immunogenicity, Vaccine, Vaccines, Virus-Like Particle immunology, Virus Assembly
- Abstract
Porcine parvovirus (PPV) is a causative agent of reproductive failure in pregnant sows. Classical inactivated vaccine is extensively used to control PPV infection, but problems concerning safety, such as incomplete inactivation may occur. In this study, a novel subunit vaccine against PPV based on virus-like particles (VLPs) formed from the complete PPV VP2 protein expressed in a prokaryotic system with co-expressed chaperones is reported. The VLPs have a similar size, shape, and hemagglutination property to the PPV. Immunization with these VLPs stimulated the neutralization antibody and hemagglutination inhibition (HI) antibody responses in mice and guinea pigs. The lymphocyte proliferation response and cytokine secretion was also induced in immunized guinea pigs comparable to those immunized with PPV inactivated vaccine. In addition, immunization with VLPs also significantly reduced the PPV content in the spleen of guinea pigs 14 days after the challenge with intact virus. These studies suggest that PPV VLPs created as described here could be a potential candidate for vaccine development., (Copyright © 2017 Elsevier B.V. All rights reserved.)
- Published
- 2017
- Full Text
- View/download PDF
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