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Hepatitis B Virus Genotype G forms core-like particles with unique structural properties.

Cotelesage JJ, Osiowy C, Lawrence C, DeVarennes SL, Teow S, Beniac DR, Booth TF - J. Viral Hepat. (2011)

Bottom Line: This results in a twelve amino acid insertion at the N-terminal end of the core protein, and two stop codons in the precore region that prevent the expression of HBeAg.We show that the position of the insertion would not interfere with translocation of nucleic acids through the pores to the core interior compartment.However, the insertion may partially obscure several residues on the core surface that are known to play a role in envelopment and secretion of virions, or that could affect structural rearrangements that may trigger envelopment after DNA second-strand synthesis.

View Article: PubMed Central - PubMed

Affiliation: Viral Diseases Division, National Microbiology Laboratory, Public Health Agency of Canada, Winnipeg, Manitoba, Canada.

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Related in: MedlinePlus

Surface shaded representation of the HBV/A capsid structure solved by X-ray crystallography (yellow), and HBV/G capsid structure solved by cryoEM (green) are shown in (a) and (b), respectively. Structures are Fourier filtered to 14 Å resolution for comparison. A difference map (c, shown in blue) was created by subtracting the HBV/A capsid structure from the HBV/G core structure is presented with a mass threshold set to account for the 12 extra residues from the HBV/G cryo-EM map. Panel (d) shows the difference map (blue) superimposed over the HBV/A core crystal structure (yellow). In all four panels, a red oval has been superposed over the reconstruction to highlight a single dimer spike in the structures at the base of the spike.
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fig02: Surface shaded representation of the HBV/A capsid structure solved by X-ray crystallography (yellow), and HBV/G capsid structure solved by cryoEM (green) are shown in (a) and (b), respectively. Structures are Fourier filtered to 14 Å resolution for comparison. A difference map (c, shown in blue) was created by subtracting the HBV/A capsid structure from the HBV/G core structure is presented with a mass threshold set to account for the 12 extra residues from the HBV/G cryo-EM map. Panel (d) shows the difference map (blue) superimposed over the HBV/A core crystal structure (yellow). In all four panels, a red oval has been superposed over the reconstruction to highlight a single dimer spike in the structures at the base of the spike.

Mentions: Superficially, the three-dimensional structure of the T = 4 capsid formed by HBV/G core protein looks very similar to the crystal structure of the HBV/A capsid, PDB accession 1QGT (Figs 2a,b) [4]. The difference map created shows additional mass around the base of the spikes of the HBV core protomers (Figs 2c,d). When the difference map is superimposed with the HBV/A atomic coordinates the additional mass of the HBV/G structure is found to be adjacent to the N-terminal residues of the core protein (Fig. 2d and Figs 3a, b). The extra mass protrudes from the surface of the core particle and sits beside the capsid pores and not over them, so this feature would not effectively reduce the diffusive movement of nucleotide triphosphates into the core interior, or affect the release of nucleic acids from the core (Fig. 3a, b). When modelling the extra 12 residues by TASSER/COOT, it was apparent that there are a number of possible arrangements that 12 residues can take up and still be contained within the corresponding density (Fig. 3c). Previously, a crystal structure of an HBV capsid protein engineered with an additional 11 residue extension to its N-terminal end has been determined, PDB accession 2QIJ [21]. Although the orientation was different from that observed in HBV/G, both additional masses were pointing away from the four-helix bundle as opposed to interacting with the main body of the core protein (Fig. 3c).


Hepatitis B Virus Genotype G forms core-like particles with unique structural properties.

Cotelesage JJ, Osiowy C, Lawrence C, DeVarennes SL, Teow S, Beniac DR, Booth TF - J. Viral Hepat. (2011)

Surface shaded representation of the HBV/A capsid structure solved by X-ray crystallography (yellow), and HBV/G capsid structure solved by cryoEM (green) are shown in (a) and (b), respectively. Structures are Fourier filtered to 14 Å resolution for comparison. A difference map (c, shown in blue) was created by subtracting the HBV/A capsid structure from the HBV/G core structure is presented with a mass threshold set to account for the 12 extra residues from the HBV/G cryo-EM map. Panel (d) shows the difference map (blue) superimposed over the HBV/A core crystal structure (yellow). In all four panels, a red oval has been superposed over the reconstruction to highlight a single dimer spike in the structures at the base of the spike.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3116152&req=5

fig02: Surface shaded representation of the HBV/A capsid structure solved by X-ray crystallography (yellow), and HBV/G capsid structure solved by cryoEM (green) are shown in (a) and (b), respectively. Structures are Fourier filtered to 14 Å resolution for comparison. A difference map (c, shown in blue) was created by subtracting the HBV/A capsid structure from the HBV/G core structure is presented with a mass threshold set to account for the 12 extra residues from the HBV/G cryo-EM map. Panel (d) shows the difference map (blue) superimposed over the HBV/A core crystal structure (yellow). In all four panels, a red oval has been superposed over the reconstruction to highlight a single dimer spike in the structures at the base of the spike.
Mentions: Superficially, the three-dimensional structure of the T = 4 capsid formed by HBV/G core protein looks very similar to the crystal structure of the HBV/A capsid, PDB accession 1QGT (Figs 2a,b) [4]. The difference map created shows additional mass around the base of the spikes of the HBV core protomers (Figs 2c,d). When the difference map is superimposed with the HBV/A atomic coordinates the additional mass of the HBV/G structure is found to be adjacent to the N-terminal residues of the core protein (Fig. 2d and Figs 3a, b). The extra mass protrudes from the surface of the core particle and sits beside the capsid pores and not over them, so this feature would not effectively reduce the diffusive movement of nucleotide triphosphates into the core interior, or affect the release of nucleic acids from the core (Fig. 3a, b). When modelling the extra 12 residues by TASSER/COOT, it was apparent that there are a number of possible arrangements that 12 residues can take up and still be contained within the corresponding density (Fig. 3c). Previously, a crystal structure of an HBV capsid protein engineered with an additional 11 residue extension to its N-terminal end has been determined, PDB accession 2QIJ [21]. Although the orientation was different from that observed in HBV/G, both additional masses were pointing away from the four-helix bundle as opposed to interacting with the main body of the core protein (Fig. 3c).

Bottom Line: This results in a twelve amino acid insertion at the N-terminal end of the core protein, and two stop codons in the precore region that prevent the expression of HBeAg.We show that the position of the insertion would not interfere with translocation of nucleic acids through the pores to the core interior compartment.However, the insertion may partially obscure several residues on the core surface that are known to play a role in envelopment and secretion of virions, or that could affect structural rearrangements that may trigger envelopment after DNA second-strand synthesis.

View Article: PubMed Central - PubMed

Affiliation: Viral Diseases Division, National Microbiology Laboratory, Public Health Agency of Canada, Winnipeg, Manitoba, Canada.

Show MeSH
Related in: MedlinePlus