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Title: Crystallization and X-ray analysis of the T = 4 particle of hepatitis B capsid protein with an N-terminal extension

Abstract

Hepatitis B virus capsids have significant potential as carriers for immunogenic peptides. The crystal structure of the T = 4 particle of hepatitis B core protein containing an N-terminal extension reveals that the fusion peptide is exposed on the exterior of the particle. Hepatitis B core (HBc) particles have been extensively exploited as carriers for foreign immunological epitopes in the development of multicomponent vaccines and diagnostic reagents. Crystals of the T = 4 HBc particle were grown in PEG 20 000, ammonium sulfate and various types of alcohols. A temperature jump from 277 or 283 to 290 K was found to enhance crystal growth. A crystal grown using MPD as a cryoprotectant diffracted X-rays to 7.7 Å resolution and data were collected to 99.6% completeness at 8.9 Å. The crystal belongs to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 352.3, b = 465.5, c = 645.0 Å. The electron-density map reveals a protrusion that is consistent with the N-terminus extending out from the surface of the capsid. The structure presented here supports the idea that N-terminal insertions can be exploited in the development of diagnostic reagents, multicomponent vaccines and delivery vehicles into mammalian cells.

Authors:
 [1]; ; ;  [2];  [3]
  1. Department of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400 Serdang, Selangor (Malaysia)
  2. Institute of Structural and Molecular Biology, School of Biological Sciences, University of Edinburgh, Michael Swann Building, King’s Buildings, Mayfield Road, Edinburgh EH9 3JR,Scotland (United Kingdom)
  3. (Malaysia)
Publication Date:
OSTI Identifier:
22360378
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal Issue: Pt 8; Other Information: PMCID: PMC2335152; PMID: 17671358; PUBLISHER-ID: bw5185; OAI: oai:pubmedcentral.nih.gov:2335152; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; AMMONIUM SULFATES; CARRIERS; CRYSTAL GROWTH; CRYSTAL STRUCTURE; CRYSTALLIZATION; CRYSTALS; DELIVERY; DENSITY; ELECTRON DENSITY; POTENTIALS; RESOLUTION; SPACE GROUPS; SURFACES

Citation Formats

Tan, Wen Siang, McNae, Iain W., Ho, Kok Lian, Walkinshaw, Malcolm D., E-mail: m.walkinshaw@ed.ac.uk, and Department of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400 Serdang, Selangor. Crystallization and X-ray analysis of the T = 4 particle of hepatitis B capsid protein with an N-terminal extension. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107033726.
Tan, Wen Siang, McNae, Iain W., Ho, Kok Lian, Walkinshaw, Malcolm D., E-mail: m.walkinshaw@ed.ac.uk, & Department of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400 Serdang, Selangor. Crystallization and X-ray analysis of the T = 4 particle of hepatitis B capsid protein with an N-terminal extension. United Kingdom. doi:10.1107/S1744309107033726.
Tan, Wen Siang, McNae, Iain W., Ho, Kok Lian, Walkinshaw, Malcolm D., E-mail: m.walkinshaw@ed.ac.uk, and Department of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400 Serdang, Selangor. Wed . "Crystallization and X-ray analysis of the T = 4 particle of hepatitis B capsid protein with an N-terminal extension". United Kingdom. doi:10.1107/S1744309107033726.
@article{osti_22360378,
title = {Crystallization and X-ray analysis of the T = 4 particle of hepatitis B capsid protein with an N-terminal extension},
author = {Tan, Wen Siang and McNae, Iain W. and Ho, Kok Lian and Walkinshaw, Malcolm D., E-mail: m.walkinshaw@ed.ac.uk and Department of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400 Serdang, Selangor},
abstractNote = {Hepatitis B virus capsids have significant potential as carriers for immunogenic peptides. The crystal structure of the T = 4 particle of hepatitis B core protein containing an N-terminal extension reveals that the fusion peptide is exposed on the exterior of the particle. Hepatitis B core (HBc) particles have been extensively exploited as carriers for foreign immunological epitopes in the development of multicomponent vaccines and diagnostic reagents. Crystals of the T = 4 HBc particle were grown in PEG 20 000, ammonium sulfate and various types of alcohols. A temperature jump from 277 or 283 to 290 K was found to enhance crystal growth. A crystal grown using MPD as a cryoprotectant diffracted X-rays to 7.7 Å resolution and data were collected to 99.6% completeness at 8.9 Å. The crystal belongs to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 352.3, b = 465.5, c = 645.0 Å. The electron-density map reveals a protrusion that is consistent with the N-terminus extending out from the surface of the capsid. The structure presented here supports the idea that N-terminal insertions can be exploited in the development of diagnostic reagents, multicomponent vaccines and delivery vehicles into mammalian cells.},
doi = {10.1107/S1744309107033726},
journal = {Acta Crystallographica. Section F},
number = Pt 8,
volume = 63,
place = {United Kingdom},
year = {Wed Aug 01 00:00:00 EDT 2007},
month = {Wed Aug 01 00:00:00 EDT 2007}
}