scholarly journals Synthesis of empty capsid-like particles of Asia I foot-and-mouth disease virus in insect cells and their immunogenicity in guinea pigs

2009 ◽  
Vol 137 (1-2) ◽  
pp. 10-17 ◽  
Author(s):  
Yimei Cao ◽  
Zengjun Lu ◽  
Jiachuan Sun ◽  
Xingwen Bai ◽  
Pu Sun ◽  
...  
Keyword(s):  
Disease Virus ◽  
Guinea Pigs ◽  
Insect Cells ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Empty Capsid ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals Expression and Immunogenicity of Two Recombinant Fusion Proteins Comprising Foot-and-Mouth Disease Virus Structural Protein VP1 and DC-SIGN-Binding Glycoproteins

2017 ◽  
Vol 2017 ◽  
pp. 1-9 ◽  
Author(s):  
Xinsheng Liu ◽  
Jianliang Lv ◽  
Yuzhen Fang ◽  
Peng Zhou ◽  
Yanzhen Lu ◽  
...  
Keyword(s):  
Immune Responses ◽  
Disease Virus ◽  
Fusion Proteins ◽  
Insect Cells ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Vp1 Protein ◽  
Sf9 Insect Cells ◽  
Mouth Disease Virus ◽  
Foot And Mouth

Improving vaccine immunogenicity by targeting antigens to dendritic cells has recently emerged as a new design strategy in vaccine development. In this study, the VP1 gene of foot-and-mouth disease virus (FMDV) serotype A was fused with the gene encoding human immunodeficiency virus (HIV) membrane glycoprotein gp120 or C2-V3 domain of hepatitis C virus (HCV) envelope glycoprotein E2, both of which are DC-SIGN-binding glycoproteins. After codon optimization, the VP1 protein and the two recombinant VP1-gp120 and VP1-E2 fusion proteins were expressed in Sf9 insect cells using the insect cell-baculovirus expression system. Western blotting showed that the VP1 protein and two recombinant VP1-gp120 and VP1-E2 fusion proteins were correctly expressed in the Sf9 insect cells and had good reactogenicity. Guinea pigs were then immunized with the purified proteins, and the resulting humoral and cellular immune responses were analyzed. The VP1-gp120 and VP1-E2 fusion proteins induced significantly higher specific anti-FMDV antibody levels than the VP1 protein and stronger cell-mediated immune responses. This study provides a new perspective for the development of novel FMDV subunit vaccines.

Delivery of a foot-and-mouth disease virus empty capsid subunit antigen with nonstructural protein 2B improves protection of swine

Vaccine ◽  
2008 ◽  
Vol 26 (45) ◽  
pp. 5689-5699 ◽  
Author(s):  
Lindomar Pena ◽  
Mauro Pires Moraes ◽  
Marla Koster ◽  
Thomas Burrage ◽  
Juan M. Pacheco ◽  
...  
Keyword(s):  
Disease Virus ◽  
Nonstructural Protein ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Empty Capsid ◽  
Mouth Disease Virus ◽  
Foot And Mouth

Development of Protective Immunity against Inactivated Iranian Isolate of Foot-and-Mouth Disease Virus Type O/IRN/2007 Using Gamma Ray-Irradiated Vaccine on BALB/c Mice and Guinea Pigs

Intervirology ◽  
2015 ◽  
Vol 58 (3) ◽  
pp. 190-196 ◽  
Author(s):  
Farahnaz Motamedi-Sedeh ◽  
Hoorieh Soleimanjahi ◽  
Amir Reza Jalilian ◽  
Homayoon Mahravani ◽  
Kamalodin Shafaee ◽  
...  
Keyword(s):  
Immune Responses ◽  
Disease Virus ◽  
Guinea Pigs ◽  
Gamma Ray ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Economic Losses ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Fmdv Type

Objectives: Foot-and-mouth disease virus (FMDV) causes a highly contagious disease in cloven-hoofed animals and is the most damaging disease of livestock worldwide, leading to great economic losses. The aim of this research was the inactivation of FMDV type O/IRN/1/2007 to produce a gamma ray-irradiated (GRI) vaccine in order to immunize mice and guinea pigs. Methods: In this research, the Iranian isolated FMDV type O/IRN/1/2007 was irradiated by gamma ray to prepare an inactivated whole virus antigen and formulated as a GRI vaccine with unaltered antigenic characteristics. Immune responses against this vaccine were evaluated on mice and guinea pigs. Results: The comparison of the immune responses between the GRI vaccine and conventional vaccine did not show any significant difference in neutralizing antibody titer, memory spleen T lymphocytes or IFN-γ, IL-4, IL-2 and IL-10 concentrations (p > 0.05). In contrast, there were significant differences in all of the evaluated immune factors between the two vaccinated groups of mice and negative control mice (p < 0.05). The protective dose 50 for the conventional and GRI vaccines obtained were 6.28 and 7.07, respectively, which indicated the high potency of both vaccines. Conclusion: GRI vaccine is suitable for both routine vaccination and control of FMDV in emergency outbreaks.

scholarly journals Assembly and characterization of foot-and-mouth disease virus empty capsid particles expressed within mammalian cells

2013 ◽  
Vol 94 (8) ◽  
pp. 1769-1779 ◽  
Author(s):  
Maria Gullberg ◽  
Bartosz Muszynski ◽  
Lindsey J. Organtini ◽  
Robert E. Ashley ◽  
Susan L. Hafenstein ◽  
...  
Keyword(s):  
Disease Virus ◽  
Mammalian Cells ◽  
Expression System ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Capsid Proteins ◽  
Dependent Manner ◽  
Empty Capsid ◽  
Mouth Disease Virus ◽  
Foot And Mouth

The foot-and-mouth disease virus (FMDV) structural protein precursor, P1-2A, is cleaved by the virus-encoded 3C protease (3Cpro) into the capsid proteins VP0, VP1 and VP3 (and 2A). In some systems, it is difficult to produce large amounts of these processed capsid proteins since 3Cpro can be toxic for cells. The expression level of 3Cpro activity has now been reduced relative to the P1-2A, and the effect on the yield of processed capsid proteins and their assembly into empty capsid particles within mammalian cells has been determined. Using a vaccinia-virus-based transient expression system, P1-2A (from serotypes O and A) and 3Cpro were expressed from monocistronic cDNA cassettes as P1-2A-3C, or from dicistronic cassettes with the 3Cpro expression dependent on a mutant FMDV internal ribosome entry site (IRES) (designated P1-2A-mIRES-3C). The effects of using a mutant 3Cpro with reduced catalytic activity or using two different mutant IRES elements (the wt GNRA tetraloop sequence GCGA converted, in the cDNA, to GAGA or GTTA) were analysed. For both serotypes, the P1-2A-mIRES-3C construct containing the inefficient GTTA mutant IRES produced the highest amount of processed capsid proteins. These products self-assembled to form FMDV empty capsid particles, which have a related, but distinct, morphology (as determined by electron microscopy and reconstruction) from that determined previously by X-ray crystallography. The assembled empty capsids bind, in a divalent cation-dependent manner, to the RGD-dependent integrin αvβ6, a cellular receptor for FMDV, and are recognized appropriately in serotype-specific antigen ELISAs.

scholarly journals Intranasal Immunization of Guinea Pigs with an Immunodominant Foot-and-Mouth Disease Virus Peptide Conjugate Induces Mucosal and Humoral Antibodies and Protection against Challenge

2003 ◽  
Vol 77 (13) ◽  
pp. 7486-7491 ◽  
Author(s):  
D. Fischer ◽  
D. Rood ◽  
R. W. Barrette ◽  
A. Zuwallack ◽  
E. Kramer ◽  
...  
Keyword(s):  
Disease Virus ◽  
Guinea Pigs ◽  
Neutralizing Antibodies ◽  
Immunoglobulin A ◽  
Foot And Mouth Disease ◽  
Keyhole Limpet Hemocyanin ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Nasal Secretions

ABSTRACT Guinea pigs immunized intranasally with a keyhole limpet hemocyanin-linked peptide, corresponding to the prominent G-H loop of the VP1 protein of foot-and-mouth disease virus, raised substantial levels of antipeptide and virus-neutralizing antibodies in sera and of peptide-specific secretory immunoglobulin A in nasal secretions. In groups of animals immunized intranasally without adjuvant, 86 percent were fully protected upon challenge with homotypic virus. Surprisingly, animals given the peptide conjugates plus the mucosal adjuvant cholera toxin were afforded only partial protection in that primary lesions were observed in most animals, although spread to other feet was prevented. These results indicate that intranasal inoculation with the peptide offers a potential route of vaccination against foot-and-mouth disease and may be useful for eliciting protection in the upper respiratory tracts of susceptible animals.

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