scholarly journals Immunogenicity evaluation of MS2 phage-mediated chimeric nanoparticle displaying an immunodominant B cell epitope of foot-and-mouth disease virus

PeerJ ◽  
2018 ◽  
Vol 6 ◽  
pp. e4823 ◽  
Author(s):  
Guoqiang Wang ◽  
Yunchao Liu ◽  
Hua Feng ◽  
Yumei Chen ◽  
Suzhen Yang ◽  
...  
Keyword(s):  
Disease Virus ◽  
Cell Epitope ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Economic Losses ◽  
Peptide Epitopes ◽  
Serotype O ◽  
Mouth Disease Virus ◽  
Foot And Mouth

Foot-and-mouth disease (FMD) is a highly contagious disease of cloven-hoofed animals that has caused tremendous economic losses worldwide. In this study, we designed a chimeric nanoparticles (CNPs) vaccine that displays the predominant epitope of the serotype O foot-and-mouth disease virus (FMDV) VP1 131-160 on the surface of MS2 phage. The recombinant protein was expressed inEscherichia Coliand can self-assemble into CNPs with diameter at 25–30 nmin vitro. A tandem repeat peptide epitopes (TRE) was prepared as control. Mice were immunized with CNPs, TRE and commercialized synthetic peptide vaccines (PepVac), respectively. The ELISA results showed that CNPs stimulated a little higher specific antibody levels to PepVac, but was significantly higher than the TRE groups. Moreover, the results from specific IFN-γ responses and lymphocyte proliferation test indicated that CNP immunized mice exhibited significantly enhanced cellular immune response compared to TRE. These results suggested that the CNPs constructed in current study could be a potential alternative vaccine in future FMDV control.

scholarly journals Immunogenicity evaluation of MS2 phage-mediated chimeric nanoparticle displaying an immunodominant B cell epitope of foot-and-mouth disease virus

2018 ◽  
Author(s):  
Guoqiang Wang ◽  
Yunchao Liu ◽  
Hua Feng ◽  
Yumei Chen ◽  
Suzhen Yang ◽  
...  
Keyword(s):  
Cell Epitope ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Economic Losses ◽  
Peptide Epitopes ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Lymphocyte Proliferation Test ◽  
Cellular Immune ◽  
Antibody Levels

Foot-and-mouth disease (FMD) is a highly contagious disease of cloven-hoofed animals that has caused tremendous economic losses worldwide. In this study, we designed a chimeric nanoparticles vaccine with the predominant epitope of FMDV (VP1 131–160) displayed on the top of the coat protein (CP) of MS2 phage. The recombinant protein was expressed in E. coli and can self-assembled into chimeric nanoparticles (CNPs) with diameter 20-25nm. A tandem repeat peptide epitopes (VP1 131–160) (TRE) was prepared as control. Mice immunized with CNPs and TRE respectively and immunogenicity evaluated show that CNPs stimulated equivalent specific antibody levels to commercialized synthetic peptide vaccines (PepVac), but was significantly higher than TRE groups. Moreover, results from specific IFN-γ responses and lymphocyte proliferation test indicated that CNPs immunized mice exhibited significantly enhanced cellular immune response. These studies suggested that the CNPs constructed in current study could be a potential alternative vaccine in future FMDV control.

A mutant of Asia 1 serotype of Foot-and-mouth disease virus with the deletion of an important antigenic epitope in the 3A protein

2011 ◽  
Vol 57 (3) ◽  
pp. 169-176 ◽  
Author(s):  
Shuang Li ◽  
Mingchun Gao ◽  
Runxiang Zhang ◽  
Ge Song ◽  
Jun Song ◽  
...  
Keyword(s):  
Disease Virus ◽  
Nonstructural Protein ◽  
Cell Epitope ◽  
Foot And Mouth Disease ◽  
Viral Disease ◽  
In Vitro Transcription ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Foot And Mouth

Foot-and-mouth disease is a highly contagious viral disease of cloven-hoofed animals. The availability of a vaccine for differentiating infected from vaccinated animals (DIVA) is crucial for the control and eradication of Foot-and-mouth disease virus (FMDV). Because traditional inactivated vaccines may contain trace nonstructural proteins interfering with the DIVA, we hypothesized that mutant FMDV with deletion of immunodominant epitopes may be valuable. Our previous study has generated a full-length cDNA clone (pBSAs) of FMDV serotype Asia 1 isolated in China. In this study, a B-cell epitope was identified in the 3A region of a nonstructural protein (NSP) by anti-FMDV cattle sera. Furthermore, we generated recombinant FMDV (rvAs-3A14D) by selectively deleting 14 amino acids (position 91–104) in the 3A region of the NSP. Following in vitro transcription and transfection in BHK-21 cells, we successfully rescued the rvAs-3A14D from BHK-21 cells. Characterization of the rvAs-3A14D revealed that the infectivity, antigenicity, and replication kinetics in BHK-21 cells and virulence in mice of the rvAs-3A14D were similar to that of its parent virus. Notably, the mutant rvAs-3A14D only replicated well in BHK-21 but did poorly in primary calf kidney cells. These data suggest that the recombinant FMDV with deletion of this epitope in the NSP may be potentially used as a candidate inactivated vaccine. Therefore, the application of the marker vaccine and differential diagnostic tests may open a promising new avenue for the development of a vaccine for DIVA.

scholarly journals Immunogenicity evaluation of MS2 phage-mediated chimeric nanoparticle displaying an immunodominant B cell epitope of foot-and-mouth disease virus

2018 ◽  
Author(s):  
Guoqiang Wang ◽  
Yunchao Liu ◽  
Hua Feng ◽  
Yumei Chen ◽  
Suzhen Yang ◽  
...  
Keyword(s):  
Cell Epitope ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Economic Losses ◽  
Peptide Epitopes ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Lymphocyte Proliferation Test ◽  
Cellular Immune ◽  
Antibody Levels

Foot-and-mouth disease (FMD) is a highly contagious disease of cloven-hoofed animals that has caused tremendous economic losses worldwide. In this study, we designed a chimeric nanoparticles vaccine with the predominant epitope of FMDV (VP1 131–160) displayed on the top of the coat protein (CP) of MS2 phage. The recombinant protein was expressed in E. coli and can self-assembled into chimeric nanoparticles (CNPs) with diameter 20-25nm. A tandem repeat peptide epitopes (VP1 131–160) (TRE) was prepared as control. Mice immunized with CNPs and TRE respectively and immunogenicity evaluated show that CNPs stimulated equivalent specific antibody levels to commercialized synthetic peptide vaccines (PepVac), but was significantly higher than TRE groups. Moreover, results from specific IFN-γ responses and lymphocyte proliferation test indicated that CNPs immunized mice exhibited significantly enhanced cellular immune response. These studies suggested that the CNPs constructed in current study could be a potential alternative vaccine in future FMDV control.

Antiviral potential of ivermectin against foot-and-mouth disease virus, serotype O, A and Asia-1

2021 ◽  
pp. 104914
Author(s):  
Zahra Naeem ◽  
Sohail Raza ◽  
Saba Afzal ◽  
Ali Ahmad Sheikh ◽  
Muhammad Muddassir Ali ◽  
...  
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Serotype O ◽  
Mouth Disease Virus ◽  
Virus Serotype ◽  
Foot And Mouth

scholarly journals Factors Required for the Uridylylation of the Foot-and-Mouth Disease Virus 3B1, 3B2, and 3B3 Peptides by the RNA-Dependent RNA Polymerase (3Dpol) In Vitro

2005 ◽  
Vol 79 (12) ◽  
pp. 7698-7706 ◽  
Author(s):  
Arabinda Nayak ◽  
Ian G. Goodfellow ◽  
Graham J. Belsham
Keyword(s):  
Rna Polymerase ◽  
Disease Virus ◽  
Rna Synthesis ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Coding Region ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Positive Strand Rna

ABSTRACT The 5′ terminus of picornavirus genomic RNA is covalently linked to the virus-encoded peptide 3B (VPg). Foot-and-mouth disease virus (FMDV) is unique in encoding and using 3 distinct forms of this peptide. These peptides each act as primers for RNA synthesis by the virus-encoded RNA polymerase 3Dpol. To act as the primer for positive-strand RNA synthesis, the 3B peptides have to be uridylylated to form VPgpU(pU). For certain picornaviruses, it has been shown that this reaction is achieved by the 3Dpol in the presence of the 3CD precursor plus an internal RNA sequence termed a cis-acting replication element (cre). The FMDV cre has been identified previously to be within the 5′ untranslated region, whereas all other picornavirus cre structures are within the viral coding region. The requirements for the in vitro uridylylation of each of the FMDV 3B peptides has now been determined, and the role of the FMDV cre (also known as the 3B-uridylylation site, or bus) in this reaction has been analyzed. The poly(A) tail does not act as a significant template for FMDV 3B uridylylation.

scholarly journals Foot-and-mouth disease virus non-structural protein 3A modulates cellular innate immune responses to influence host tropism

2020 ◽  
Vol 2 (7A) ◽  
Author(s):  
Soumendu Chakravarti ◽  
Caroline Wright ◽  
Emma Howes ◽  
Richard Kock ◽  
Terry Jackson ◽  
...  
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Economic Losses ◽  
Structural Protein ◽  
Host Tropism ◽  
C Terminus ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Species Specific

The picornavirus foot-and-mouth disease virus (FMDV) is responsible for one of the most significant diseases of livestock, leading to large economic losses due to reduced productivity and trade embargoes for areas not certified as disease-free. The picornavirus non-structural protein 3A is involved in replication of the viral RNA genome and is implicated in host tropism of several picornaviruses. Deletions in the C-terminus of 3A have been observed in FMDV outbreaks specific for swine and such viruses are non-pathogenic in cattle. The mechanism for species specific attenuation of FMDV is unknown. We have shown that FMDV containing a C-terminal deletion in 3A is attenuated in bovine cell culture and that the attenuated phenotype can be reversed by the JAK1/2 inhibitor Ruxolitinib (Rux), identifying a role for the induction of interferon stimulated genes (ISGs) in the restricted bovine tropism of the 3A-deleted virus.

scholarly journals Lithium chloride inhibits early stages of foot-and-mouth disease virus (FMDV) replication in vitro

2017 ◽  
Vol 89 (11) ◽  
pp. 2041-2046 ◽  
Author(s):  
Fu-Rong Zhao ◽  
Yin-Li Xie ◽  
Ze-Zhong Liu ◽  
Jun-Jun Shao ◽  
Shi-Fang Li ◽  
...  
Keyword(s):  
Disease Virus ◽  
Lithium Chloride ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Early Stages ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Fmdv Replication

scholarly journals Impairment of the DeISGylation Activity of Foot-and-Mouth Disease Virus Lpro Causes Attenuation In Vitro and In Vivo

2020 ◽  
Vol 94 (13) ◽  
Author(s):  
Gisselle N. Medina ◽  
Paul Azzinaro ◽  
Elizabeth Ramirez-Medina ◽  
Joseph Gutkoska ◽  
Ying Fang ◽  
...  
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Type I ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Infected Cells ◽  
Viral Attenuation

ABSTRACT Foot-and-mouth disease virus (FMDV) leader proteinase (Lpro) affects several pathways of the host innate immune response. Previous studies in bovine cells demonstrated that deletions (leaderless [LLV]) or point mutations in Lpro result in increased expression of interferon (IFN) and IFN-stimulated genes (ISGs), including, among others, the ubiquitin-like protein modifier ISG15 and the ubiquitin specific peptidase USP18. In addition to its conventional papain-like protease activity, Lpro acts as a deubiquitinase (DUB) and deISGylase. In this study, we identified a conserved residue in Lpro that is involved in its interaction with ISG15. Mutation W105A rendered Escherichia coli-expressed Lpro unable to cleave the synthetic substrate pro-ISG15 while preserving cellular eIF4G cleavage. Interestingly, mutant FMDV W105A was viable. Overexpression of ISG15 and the ISGylation machinery in porcine cells resulted in moderate inhibition of FMDV replication, along with a decrease of the overall state of ISGylation in wild-type (WT)-infected cells. In contrast, reduced deISGylation was observed upon infection with W105A and leaderless virus. Reduction in the levels of deubiquitination was also observed in cells infected with the FMDV LproW105A mutant. Surprisingly, similarly to WT, infection with W105A inhibited IFN/ISG expression despite displaying an attenuated phenotype in vivo in mice. Altogether, our studies indicate that abolishing/reducing the deISGylase/DUB activity of Lpro causes viral attenuation independently of its ability to block the expression of IFN and ISG mRNA. Furthermore, our studies highlight the potential of ISG15 to be developed as a novel biotherapeutic molecule against FMD. IMPORTANCE In this study, we identified an aromatic hydrophobic residue in foot-and-mouth disease virus (FMDV) leader proteinase (Lpro) (W105) that is involved in the interaction with ISG15. Mutation in Lpro W105 (A12-LproW105A) resulted in reduced deISGylation in vitro and in porcine-infected cells. Impaired deISGylase activity correlated with viral attenuation in vitro and in vivo and did not affect the ability of Lpro to block expression of type I interferon (IFN) and other IFN-stimulated genes. Moreover, overexpression of ISG15 resulted in the reduction of FMDV viral titers. Thus, our study highlights the potential use of Lpro mutants with modified deISGylase activity for development of live attenuated vaccine candidates, and ISG15 as a novel biotherapeutic against FMD.

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