Structure of Foot-and-Mouth Disease Virus Particles

2004 ◽  
pp. 78-92
Author(s):  
Ignacio Fita ◽  
Cristina Ferrer-Dria
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Virus Particles ◽  
Mouth Disease Virus ◽  
Foot And Mouth

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

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.

Epitopes on foot-and-mouth disease virus particles I. Topology

Virology ◽  
1987 ◽  
Vol 157 (2) ◽  
pp. 516-525 ◽  
Author(s):  
K.C. McCullough ◽  
J.R. Crowther ◽  
W.C. Carpenter ◽  
E. Brocchi ◽  
L. Capucci ◽  
...  
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Virus Particles ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals Foot-and-mouth disease virus particles contain replicase protein 3D.

1994 ◽  
Vol 91 (2) ◽  
pp. 733-737 ◽  
Author(s):  
J. F. Newman ◽  
P. G. Piatti ◽  
B. M. Gorman ◽  
T. G. Burrage ◽  
M. D. Ryan ◽  
...  
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Virus Particles ◽  
Replicase Protein ◽  
Mouth Disease Virus ◽  
Foot And Mouth

Analysis of SAT1 type foot-and-mouth disease virus capsid proteins: Influence of receptor usage on the properties of virus particles

2011 ◽  
Vol 155 (2) ◽  
pp. 462-472 ◽  
Author(s):  
Francois F. Maree ◽  
Belinda Blignaut ◽  
Lisa Aschenbrenner ◽  
Tom Burrage ◽  
Elizabeth Rieder
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Capsid Proteins ◽  
Virus Capsid ◽  
Virus Particles ◽  
Receptor Usage ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals Evidence for a Group Protein in Foot-and-Mouth Disease Virus Particles

1973 ◽  
Vol 19 (3) ◽  
pp. 369-380 ◽  
Author(s):  
P. Talbot ◽  
D. J. Rowlands ◽  
J. N. Burroughs ◽  
D. V. Sangar ◽  
F. Brown
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Virus Particles ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Group Protein

scholarly journals A study of the heterogeneous 37s ribonucleic acid induced by foot-and-mouth-disease virus

1968 ◽  
Vol 107 (3) ◽  
pp. 395-401 ◽  
Author(s):  
T. F. Wild ◽  
S J Martin ◽  
F. Brown
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Kidney Cells ◽  
Virus Particles ◽  
Mouth Disease Virus ◽  
Heterogeneous Nature ◽  
Foot And Mouth ◽  
Sepharose 4B ◽  
Baby Hamster Kidney Cells

1. The 37s RNA induced in baby-hamster kidney cells by infection with foot-and-mouth-disease virus was examined on sucrose gradients and by filtration through Sepharose 4B. 2. The RNA sedimented faster (37s) and as a broader band than the 35s RNA from purified virus. 3. Treatment with deoxyribonuclease, Pronase or amylase did not alter the sedimentation profile of the 37s RNA. 4. Treatment of individual fractions of the RNA with phenol, dimethyl sulphoxide or methylCellosolve did not decrease the sedimentation rate of the faster-sedimenting molecules. 5. Sedimentation in sucrose gradients of different ionic strengths or containing EDTA had no effect on the heterogeneous nature of the profile. 6. On filtration through Sepharose 4B columns, the 37s virus-induced RNA was eluted before viral RNA. 7. Only 20% of the rapidly sedimenting RNA was incorporated into complete virus particles.

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