Research on Measures of Reducing Environmental Pollutions by Empty Capsid Virus Particles with Vaccine of Foot and Mouth Disease Virus to Control FMD

2014 ◽  
Vol 1023 ◽  
pp. 257-261
Author(s):  
Qi Hong ◽  
Zi Hong Liu ◽  
Duan Dan Han
Keyword(s):  
Virus Particle ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Promising Candidate ◽  
Effective Measure ◽  
Virus Particles ◽  
Empty Capsid ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Potential Benefits

Foot-and-mouth disease (FMD) is a highly contagious disease in cloven-hoofed animals, and had been broken out worldwide several times in recent years. In order to extinct outbreak of FMD, a large number of infected animals are slaughtered in some countries, and the slaughterings had been caused a series of environmental pollutions seriously. To reduce this kind of pollution, vaccination is an effective measure to protect animals against FMD, however, FMD virus (FMDV) escaping from manufacturing plant and inactivated incompletely during vaccine production could cause an outbreak of FMD. Therefore, inactivated FMDV vaccines are not safe to animals and environment. FMDV empty capsid (lacking nucleic acid) can elicit the same antibody response as infectious FMDV, thus, empty capsid virus particle vaccine of FMDV would be the most promising candidate vaccine for its safety and protection against FMDV. In this report, we studied the empty capsid virus particle vaccine of FMDV to control FMD and its potential benefits to the environment.

Foot-and-mouth disease virus particles inactivated with binary ethylenimine are efficiently internalized into cultured cells

Vaccine ◽  
2011 ◽  
Vol 29 (52) ◽  
pp. 9655-9662 ◽  
Author(s):  
Miguel A. Martín-Acebes ◽  
Ángela Vázquez-Calvo ◽  
Mónica González-Magaldi ◽  
Francisco Sobrino
Keyword(s):  
Disease Virus ◽  
Cultured Cells ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Virus Particles ◽  
Mouth Disease Virus ◽  
Foot And Mouth

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

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 A review of the possible mechanisms for the persistence of foot-and-mouth disease virus

1995 ◽  
Vol 114 (1) ◽  
pp. 1-13 ◽  
Author(s):  
E. L. Woodbury
Keyword(s):  
Virus Particle ◽  
Disease Virus ◽  
Infectious Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Animal Disease ◽  
Mouth Disease Virus ◽  
Positive Sense ◽  
Foot And Mouth ◽  
Single Polypeptide

Foot-and-mouth disease (FMD) was the first animal disease to be attributed to a virus, and the second virus to be discovered [1]. It is a positive-sense, singlestranded RNA picornavirus and the sole member of the genus Aphthovirus. Each infectious virus particle contains a single strand of RNA approximately 8-5 kb long. This is translated into a single polypeptide which is then cleaved into the structural and non-structural virus proteins.

scholarly journals Sequence adaptations affecting cleavage of the VP1/2A junction by the 3C protease in foot-and-mouth disease virus-infected cells

2014 ◽  
Vol 95 (11) ◽  
pp. 2402-2410 ◽  
Author(s):  
Maria Gullberg ◽  
Charlotta Polacek ◽  
Graham J. Belsham
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Single Amino Acid ◽  
Virus Particles ◽  
3C Protease ◽  
Serotype O ◽  
Single Amino Acid Residue ◽  
Mouth Disease Virus ◽  
Foot And Mouth

The foot-and-mouth disease virus (FMDV) capsid protein precursor P1-2A is cleaved by the virus-encoded 3C protease to VP0, VP3, VP1 and 2A. It was shown previously that modification of a single amino acid residue (K210E) within the VP1 protein and close to the VP1/2A cleavage site, inhibited cleavage of this junction and produced ‘self-tagged’ virus particles. A second site substitution (E83K) within VP1 was also observed within the rescued virus [Gullberg et al. (2013). J Virol 87, 11591–11603]. It was shown here that introduction of this E83K change alone into a serotype O virus resulted in the rapid accumulation of a second site substitution within the 2A sequence (L2P), which also blocked VP1/2A cleavage. This suggests a linkage between the E83K change in VP1 and cleavage of the VP1/2A junction. Cells infected with viruses containing the VP1 K210E or the 2A L2P substitutions contained the uncleaved VP1-2A protein. The 2A L2P substitution resulted in the VP1/2A junction being highly resistant to cleavage by the 3C protease, hence it may be a preferred route for ‘tagging’ virus particles.

Sign in / Sign up

Export Citation Format

Share Document