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An N-terminal extension to the hepatitis B virus core protein forms a poorly ordered trimeric spike in assembled virus-like particles

Research output: Contribution to Journal/Magazine › Journal article › peer-review

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An N-terminal extension to the hepatitis B virus core protein forms a poorly ordered trimeric spike in assembled virus-like particles. / McGonigle, Richard; Yap, Wei Boon; Ong, Swee Tin et al.
In: Journal of Structural Biology, Vol. 189, No. 2, 02.2015, p. 73-80.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

McGonigle, R, Yap, WB, Ong, ST, Gatherer, D, Bakker, SE, Tan, WS & Bhella, D 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, vol. 189, no. 2, pp. 73-80. https://doi.org/10.1016/j.jsb.2014.12.006

APA

McGonigle, R., Yap, W. B., Ong, S. T., Gatherer, D., Bakker, S. E., Tan, W. S., & Bhella, D. (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), 73-80. https://doi.org/10.1016/j.jsb.2014.12.006

Vancouver

McGonigle R, Yap WB, Ong ST, Gatherer D, Bakker SE, Tan WS et al. 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. 2015 Feb;189(2):73-80. Epub 2014 Dec 31. doi: 10.1016/j.jsb.2014.12.006

Author

McGonigle, Richard ; Yap, Wei Boon ; Ong, Swee Tin et al. / An N-terminal extension to the hepatitis B virus core protein forms a poorly ordered trimeric spike in assembled virus-like particles. In: Journal of Structural Biology. 2015 ; Vol. 189, No. 2. pp. 73-80.

Bibtex

@article{e1b99775ad84465f8afa89f33c3561a2,
title = "An N-terminal extension to the hepatitis B virus core protein forms a poorly ordered trimeric spike in assembled virus-like particles",
abstract = "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.",
keywords = "Virus-like particle, Vaccine, Hepatitis B virus , Cryo-electron microscopy , Three-dimensional reconstruction, Local resolution",
author = "Richard McGonigle and Yap, {Wei Boon} and Ong, {Swee Tin} and Derek Gatherer and Bakker, {Saskia E} and Tan, {Wen Siang} and David Bhella",
note = "Copyright {\textcopyright} 2015. Published by Elsevier Inc. Open Access funded by Medical Research Council Under a Creative Commons license Date of Acceptance 24/12/2014",
year = "2015",
month = feb,
doi = "10.1016/j.jsb.2014.12.006",
language = "English",
volume = "189",
pages = "73--80",
journal = "Journal of Structural Biology",
issn = "1095-8657",
publisher = "Academic Press Inc.",
number = "2",

}

RIS

TY - JOUR

T1 - An N-terminal extension to the hepatitis B virus core protein forms a poorly ordered trimeric spike in assembled virus-like particles

AU - McGonigle, Richard

AU - Yap, Wei Boon

AU - Ong, Swee Tin

AU - Gatherer, Derek

AU - Bakker, Saskia E

AU - Tan, Wen Siang

AU - Bhella, David

N1 - Copyright © 2015. Published by Elsevier Inc. Open Access funded by Medical Research Council Under a Creative Commons license Date of Acceptance 24/12/2014

PY - 2015/2

Y1 - 2015/2

N2 - 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.

AB - 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.

KW - Virus-like particle

KW - Vaccine

KW - Hepatitis B virus

KW - Cryo-electron microscopy

KW - Three-dimensional reconstruction

KW - Local resolution

U2 - 10.1016/j.jsb.2014.12.006

DO - 10.1016/j.jsb.2014.12.006

M3 - Journal article

C2 - 25557498

VL - 189

SP - 73

EP - 80

JO - Journal of Structural Biology

JF - Journal of Structural Biology

SN - 1095-8657

IS - 2

ER -