An N-terminal extension to the hepatitis B virus core protein forms a poorly ordered trimeric spike in assembled virus-like particles
Virus-like particles composed of the core antigen of hepatitis B virus (HBcAg) have been shown to be an effective platform for the display of foreign epitopes in vaccine development. Heterologous sequences have been successfully inserted at both amino and carboxy termini as well as internally at the...
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| Format: | Article |
| Language: | English |
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Elsevier
2015
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| Online Access: | http://psasir.upm.edu.my/id/eprint/43732/1/An%20N-terminal%20extension%20to%20the%20hepatitis%20B%20virus%20core%20protein%20forms%20a%20poorly%20ordered%20.pdf |
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| author | McGonigle, Richard Wei, Boon Yap Swee, Tin Ong Gatherer, Derek Bakkera, Saskia E. Wen, Siang Tan Bhella, David |
| author_facet | McGonigle, Richard Wei, Boon Yap Swee, Tin Ong Gatherer, Derek Bakkera, Saskia E. Wen, Siang Tan Bhella, David |
| author_sort | McGonigle, Richard |
| collection | UPM |
| description | Virus-like particles composed of the core antigen of hepatitis B virus (HBcAg) have been shown to be an effective platform for the display of foreign epitopes in vaccine development. Heterologous sequences have been successfully inserted at both amino and carboxy termini as well as internally at the major immunodominant epitope. We used cryogenic electron microscopy (CryoEM) and three-dimensional image reconstruction to investigate the structure of VLPs assembled from an N-terminal extended HBcAg that contained a polyhistidine tag. The insert was seen to form a trimeric spike on the capsid surface that was poorly resolved, most likely owing to it being flexible. We hypothesise that the capacity of N-terminal inserts to form trimers may have application in the development of multivalent vaccines to trimeric antigens. Our analysis also highlights the value of tools for local resolution assessment in studies of partially disordered macromolecular assemblies by cryoEM. |
| first_indexed | 2024-03-06T08:56:32Z |
| format | Article |
| id | upm.eprints-43732 |
| institution | Universiti Putra Malaysia |
| language | English |
| last_indexed | 2024-03-06T08:56:32Z |
| publishDate | 2015 |
| publisher | Elsevier |
| record_format | dspace |
| spelling | upm.eprints-437322016-08-08T09:40:18Z http://psasir.upm.edu.my/id/eprint/43732/ An N-terminal extension to the hepatitis B virus core protein forms a poorly ordered trimeric spike in assembled virus-like particles McGonigle, Richard Wei, Boon Yap Swee, Tin Ong Gatherer, Derek Bakkera, Saskia E. Wen, Siang Tan Bhella, David Virus-like particles composed of the core antigen of hepatitis B virus (HBcAg) have been shown to be an effective platform for the display of foreign epitopes in vaccine development. Heterologous sequences have been successfully inserted at both amino and carboxy termini as well as internally at the major immunodominant epitope. We used cryogenic electron microscopy (CryoEM) and three-dimensional image reconstruction to investigate the structure of VLPs assembled from an N-terminal extended HBcAg that contained a polyhistidine tag. The insert was seen to form a trimeric spike on the capsid surface that was poorly resolved, most likely owing to it being flexible. We hypothesise that the capacity of N-terminal inserts to form trimers may have application in the development of multivalent vaccines to trimeric antigens. Our analysis also highlights the value of tools for local resolution assessment in studies of partially disordered macromolecular assemblies by cryoEM. Elsevier 2015 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/43732/1/An%20N-terminal%20extension%20to%20the%20hepatitis%20B%20virus%20core%20protein%20forms%20a%20poorly%20ordered%20.pdf McGonigle, Richard and Wei, Boon Yap and Swee, Tin Ong and Gatherer, Derek and Bakkera, Saskia E. and Wen, Siang Tan and Bhella, David (2015) An N-terminal extension to the hepatitis B virus core protein forms a poorly ordered trimeric spike in assembled virus-like particles. Journal of Structural Biology, 189 (2). pp. 73-80. ISSN 1047-8477 http://www.sciencedirect.com/science/article/pii/S1047847714002809 10.1016/j.jsb.2014.12.006 |
| spellingShingle | McGonigle, Richard Wei, Boon Yap Swee, Tin Ong Gatherer, Derek Bakkera, Saskia E. Wen, Siang Tan Bhella, David An N-terminal extension to the hepatitis B virus core protein forms a poorly ordered trimeric spike in assembled virus-like particles |
| title | An N-terminal extension to the hepatitis B virus core protein forms a poorly ordered trimeric spike in assembled virus-like particles |
| title_full | An N-terminal extension to the hepatitis B virus core protein forms a poorly ordered trimeric spike in assembled virus-like particles |
| title_fullStr | An N-terminal extension to the hepatitis B virus core protein forms a poorly ordered trimeric spike in assembled virus-like particles |
| title_full_unstemmed | An N-terminal extension to the hepatitis B virus core protein forms a poorly ordered trimeric spike in assembled virus-like particles |
| title_short | An N-terminal extension to the hepatitis B virus core protein forms a poorly ordered trimeric spike in assembled virus-like particles |
| title_sort | n terminal extension to the hepatitis b virus core protein forms a poorly ordered trimeric spike in assembled virus like particles |
| url | http://psasir.upm.edu.my/id/eprint/43732/1/An%20N-terminal%20extension%20to%20the%20hepatitis%20B%20virus%20core%20protein%20forms%20a%20poorly%20ordered%20.pdf |
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