Generation of Antibodies against Foot-and-Mouth-Disease Virus Capsid Protein VP4 Using Hepatitis B Core VLPs as a Scaffold
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 t...
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MDPI AG
2021-04-01
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| Online Access: | https://www.mdpi.com/2075-1729/11/4/338 |
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| author | Jessica Swanson Rennos Fragkoudis Philippa C. Hawes Joseph Newman Alison Burman Anusha Panjwani Nicola J. Stonehouse Tobias J. Tuthill |
| author_facet | Jessica Swanson Rennos Fragkoudis Philippa C. Hawes Joseph Newman Alison Burman Anusha Panjwani Nicola J. Stonehouse Tobias J. Tuthill |
| author_sort | Jessica Swanson |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-10T12:25:44Z |
| format | Article |
| id | doaj.art-0b56d8b0c2854872b35c69ca52c55120 |
| institution | Directory Open Access Journal |
| issn | 2075-1729 |
| language | English |
| last_indexed | 2024-03-10T12:25:44Z |
| publishDate | 2021-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Life |
| spelling | doaj.art-0b56d8b0c2854872b35c69ca52c551202023-11-21T15:03:13ZengMDPI AGLife2075-17292021-04-0111433810.3390/life11040338Generation of Antibodies against Foot-and-Mouth-Disease Virus Capsid Protein VP4 Using Hepatitis B Core VLPs as a ScaffoldJessica Swanson0Rennos Fragkoudis1Philippa C. Hawes2Joseph Newman3Alison Burman4Anusha Panjwani5Nicola J. Stonehouse6Tobias J. Tuthill7The Pirbright Institute, Pirbright GU24 0NF, UKThe Pirbright Institute, Pirbright GU24 0NF, UKThe Pirbright Institute, Pirbright GU24 0NF, UKThe Pirbright Institute, Pirbright GU24 0NF, UKThe Pirbright Institute, Pirbright GU24 0NF, UKThe Pirbright Institute, Pirbright GU24 0NF, UKFaculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UKThe Pirbright Institute, Pirbright GU24 0NF, UKThe 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.https://www.mdpi.com/2075-1729/11/4/338picornavirusFMDVVLPcapsidantibodies |
| spellingShingle | Jessica Swanson Rennos Fragkoudis Philippa C. Hawes Joseph Newman Alison Burman Anusha Panjwani Nicola J. Stonehouse Tobias J. Tuthill Generation of Antibodies against Foot-and-Mouth-Disease Virus Capsid Protein VP4 Using Hepatitis B Core VLPs as a Scaffold Life picornavirus FMDV VLP capsid antibodies |
| title | Generation of Antibodies against Foot-and-Mouth-Disease Virus Capsid Protein VP4 Using Hepatitis B Core VLPs as a Scaffold |
| title_full | Generation of Antibodies against Foot-and-Mouth-Disease Virus Capsid Protein VP4 Using Hepatitis B Core VLPs as a Scaffold |
| title_fullStr | Generation of Antibodies against Foot-and-Mouth-Disease Virus Capsid Protein VP4 Using Hepatitis B Core VLPs as a Scaffold |
| title_full_unstemmed | Generation of Antibodies against Foot-and-Mouth-Disease Virus Capsid Protein VP4 Using Hepatitis B Core VLPs as a Scaffold |
| title_short | Generation of Antibodies against Foot-and-Mouth-Disease Virus Capsid Protein VP4 Using Hepatitis B Core VLPs as a Scaffold |
| title_sort | generation of antibodies against foot and mouth disease virus capsid protein vp4 using hepatitis b core vlps as a scaffold |
| topic | picornavirus FMDV VLP capsid antibodies |
| url | https://www.mdpi.com/2075-1729/11/4/338 |
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