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. 2008;47(33):6247-51.
doi: 10.1002/anie.200802410.

Stability and shape of hepatitis B virus capsids in vacuo

Charlotte Uetrecht  1 , Cees Versluis, Norman R Watts, Paul T Wingfield, Alasdair C Steven, Albert J R Heck
Affiliations

Stability and shape of hepatitis B virus capsids in vacuo

Charlotte Uetrecht et al. Angew Chem Int Ed Engl. 2008.
No abstract available

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Figures

Figure 1
Figure 1
Ion mobility MS on HBV cp149 61C capsids. A) Mass spectrum of 61C, adapted from Uetrecht et al., 2008.[8] The distributions around m/z 22000 and 25000 represent the T = 3 and T = 4 capsids (pink and blue), respectively. For each distribution, the most abundant charge state is indicated. The inset on the right shows a spectrum deconvolved to uncharged species. The calculated monomer mass is 16706 Da. B) Contour plot of the ion mobility drift time versus m/z for 61C capsids at 0.04 µm (ca. 8 µm cp monomer) in 200 mm ammonium acetate, pH 6.8, without fragmentation (150 V accelerating voltage). Both the T = 3 (pink ellipse) and T = 4 (blue ellipse) capsids show small (purple) and large (orange) conformers.
Figure 2
Figure 2
Shape of HBV capsids in vacuo. A) Charge state distributions of the small (purple) and large (orange) T = 3 conformers as extracted from Figure 1B normalized to the intensity of their individual base signal. The inset shows the unchanged abundance and relative size of conformers, which is independent of the charge state and accelerating voltage (165+ ion at 100 V and the 169+, 165+, and 161+ ions at 150 V (dark to light blue) of 61C T = 4). The cross-sections (Ω) and intensities are normalized on the base signal of a particular charge state and overlay almost perfectly. B) Volumes derived from the cross-sections for a large set of proteins and protein complexes (circles, see also Table S2 in the Supporting Information) and the 3C→A and 61C capsids (triangles). Error bars represent the standard deviation. The small and large conformers are depicted in purple and orange, respectively. The solid line represents a linear regression in the set of globular proteins. The dashed lines correspond to a 99% confidence interval of the linear regression. The EM reconstructions[10] of T = 3 and T = 4 are shown to the left of the triangles.
Figure 3
Figure 3
Curves showing the breakdown of HBV cp149 capsids in vacuo. Abundance of undissociated T = 3 (circles) and T = 4 (triangles) capsids from: A) m/z 24 500 3C→A and B) m/z 24000 61C precursor selection at different collision voltages. The solid lines correspond to sigmoidal fits. The curve progressions are indistinguishable irrespective of whether the laboratory frame or center of mass energy is displayed in the plots.
Figure 4
Figure 4
Dissociation and cross-sections (Ω) of capsids in vacuo. A) Relative abundance of the conformers of a 141+ ion (undissociated T = 3 61C) without (150 V; dark purple) and with fragmentation (175 and 200 V; purple and pink, respectively) compared to the 126+ counterion from which one dimer was ejected (200 V, black). Cross-sections were normalized on the small conformation and intensities on the base signal. B) Cross-sections of61 C capsids for large (orange) and small (purple) conformers of undissociated T = 3 (circles) and T = 3 missing a dimer (triangles) for all the detected charge states. The linear correlation between the cross-section and charge indicates similar structures for the undissociated precursor and the fragmentation products.
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