scholarly journals Interspecies Major Histocompatibility Complex-Restricted Th Cell Epitope on Foot-and-Mouth Disease Virus Capsid Protein VP4

2000 ◽  
Vol 74 (10) ◽  
pp. 4902-4907 ◽  
Author(s):  
E. Blanco ◽  
K. McCullough ◽  
A. Summerfield ◽  
J. Fiorini ◽  
D. Andreu ◽  
...  
Keyword(s):  
Major Histocompatibility Complex ◽  
Capsid Protein ◽  
Disease Virus ◽  
Cell Epitope ◽  
Foot And Mouth Disease ◽  
Virus Capsid ◽  
Histocompatibility Complex ◽  
Th Cell ◽  
Mouth Disease Virus ◽  
Virus Capsid Protein

scholarly journals Foot-and-mouth disease virus capsid protein VP2 activates the cellular EIF2S1-ATF4 pathway and induces autophagy via HSPB1

Autophagy ◽  
2018 ◽  
Vol 14 (2) ◽  
pp. 336-346 ◽  
Author(s):  
Peng Sun ◽  
Shumin Zhang ◽  
Xiaodong Qin ◽  
Xingni Chang ◽  
Xiaorui Cui ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Virus Capsid ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Virus Capsid Protein

scholarly journals Generation of Antibodies against Foot-and-Mouth-Disease Virus Capsid Protein VP4 Using Hepatitis B Core VLPs as a Scaffold

Life ◽  
2021 ◽  
Vol 11 (4) ◽  
pp. 338
Author(s):  
Jessica Swanson ◽  
Rennos Fragkoudis ◽  
Philippa C. Hawes ◽  
Joseph Newman ◽  
Alison Burman ◽  
...  
Keyword(s):  
Amino Acids ◽  
Hepatitis B ◽  
Capsid Protein ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Specific Antibodies ◽  
Mouth Disease Virus ◽  
N Terminus ◽  
Foot And Mouth

The picornavirus foot-and-mouth disease virus (FMDV) is the causative agent of the economically important disease of livestock, foot-and-mouth disease (FMD). VP4 is a highly conserved capsid protein, which is important during virus entry. Previous published work has shown that antibodies targeting the N-terminus of VP4 of the picornavirus human rhinovirus are broadly neutralising. In addition, previous studies showed that immunisation with the N-terminal 20 amino acids of enterovirus A71 VP4 displayed on the hepatitis B core (HBc) virus-like particles (VLP) can induce cross-genotype neutralisation. To investigate if a similar neutralising response against FMDV VP4 could be generated, HBc VLPs displaying the N-terminus of FMDV VP4 were designed. The N-terminal 15 amino acids of FMDV VP4 was inserted into the major immunodominant region. HBc VLPs were also decorated with peptides of the N-terminus of FMDV VP4 attached using a HBc-spike binding tag. Both types of VLPs were used to immunise mice and the resulting serum was investigated for VP4-specific antibodies. The VLP with VP4 inserted into the spike, induced VP4-specific antibodies, however the VLPs with peptides attached to the spikes did not. The VP4-specific antibodies could recognise native FMDV, but virus neutralisation was not demonstrated. This work shows that the HBc VLP presents a useful tool for the presentation of FMDV capsid epitopes.

scholarly journals An Engineered Maturation Cleavage Provides a Recombinant Mimic of Foot-and-Mouth Disease Virus Capsid Assembly-Disassembly

Life ◽  
2021 ◽  
Vol 11 (6) ◽  
pp. 500
Author(s):  
Joseph Newman ◽  
David J. Rowlands ◽  
Tobias J. Tuthill
Keyword(s):  
Capsid Protein ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Virion Assembly ◽  
Capsid Precursor ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Assembly Intermediate ◽  
Capsid Stability

Picornavirus capsids are assembled from 60 copies of a capsid precursor via a pentameric assembly intermediate or ‘pentamer’. Upon completion of virion assembly, a maturation event induces a final cleavage of the capsid precursor to create the capsid protein VP4, which is essential for capsid stability and entry into new cells. For the picornavirus foot-and-mouth disease virus (FMDV), intact capsids are temperature and acid-labile and can disassemble into pentamers. During disassembly, capsid protein VP4 is lost, presumably altering the structure and properties of the resulting pentamers. The purpose of this study was to compare the characteristics of recombinant “assembly” and “disassembly” pentamers. We generated recombinant versions of these different pentamers containing an engineered cleavage site to mimic the maturation cleavage. We compared the sedimentation and antigenic characteristics of these pentamers using sucrose density gradients and reactivity with an antibody panel. Pentamers mimicking the assembly pathway sedimented faster than those on the disassembly pathway suggesting that for FMDV, in common with other picornaviruses, assembly pentamers sediment at 14S whereas only pentamers on the disassembly pathway sediment at 12S. The reactivity with anti-VP4 antibodies was reduced for the 12S pentamers, consistent with the predicted loss of VP4. Reactivity with other antibodies was similar for both pentamers suggesting that major antigenic features may be preserved between the VP4 containing assembly pentamers and the disassembly pentamers lacking VP4.

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