Virion Portrait
Dr. Jez Lim Marston, MD, PhD
Companion to Cracking the Glycan Shield

Virion portrait.

A mature HIV particle cut in half, drawn to scale. Look at how few spikes there are and how far apart they sit. The spike itself is the real 5FYJ structure with a full sugar coat.

~145 nm virion14 ± 7 spikes per particle5FYJ spike · 1HZH antibody← Back to the main report
Not peer reviewedThis page is part of independent computational work and has not been through peer review. I welcome scrutiny. If you work on HIV antibodies, glycan shields, or viral escape and you find an error, a questionable assumption, or a better way to test a result, please write to jezlim.marston@gmail.com.
The cut view and the outside

One virion, cut in half and seen from outside

Spikes
Show
Cut in halfFrom outside
Drag the handle (or use the arrow keys) to swap between the two halves of the same particle. The cut view removes the front half, so most spikes are hidden. The outside view is that front half seen from outside, with the same spikes in the same places. Together the two views show every spike on the particle.
One spike up close

The Env trimer up close

Glycans
Bound Fab
Copies
View
Measured and drawn

What in this picture is data

PartStatusBasis
Env spike, proteinatomic coordinatesPDB 5FYJ, three protomers, 14,967 heavy atoms1. Height and width are measured from the coordinates.
Env spike, glycansmodeledOne random draw of the Man9 shield from the full-density model (31 sites per protomer)2,3, 11,811 atoms.
Virion size, spike countliteratureMean particle size about 145 nm (Briggs et al. 20034). Average of 14 ± 7 spikes per particle (Zhu et al.5), so the 4 and 35 buttons are not extremes of the model but the spread of the data.
Spike positionsrandomPlaced at random on the sphere with a minimum spacing. Each arrangement is one possible virion; the cut view and the outside view always show the same one.
CapsiddrawnCone about 60 nm across at the wide end, 20–30 nm at the narrow end; about 1,500 CA copies in roughly 250 hexamers and 12 pentamers6. Ticks on the wall mark the 9.6 nm hexamer spacing. Length and wall thickness are approximate.
Lipids, matrix, RNA, enzymesdrawnProcedural shapes sized to be plausible, not atomic models. Bilayer thickness is about 4.6 nm in this drawing.
Antibodyatomic coordinatesPDB 1HZH, the intact human IgG1 b12 (Saphire et al. 20017), 151.6 kDa and about 15 nm across, drawn as one bead per residue plus the Fc sugars at the same scale as the spikes, both in the virion picture and in its own panel beside the spike close-up at the same scale. It is not docked to any spike, and its placement in the virion picture is a drawn choice. The amber sugars are the Fc glycans listed in 1HZH. b12 targets the CD4 binding site; it is not one of the six antibodies in this report.
Fabs on the spikeatomic coordinatesPDB 5FYJ as crystallized: PGT122 and 35O22 as full Fab chains, VRC01 as its variable domains only8,9,10. One copy per protomer, placed with the same symmetry operations as the spike. Sugars of the modeled shield that would overlap a shown Fab are hidden, which is an approximation.

The cut removes the front half of the virion, along with any spikes that sat on it, so the picture shows only the spikes on the back half. Spike structure and glycan model come from the same work as the epitope atlas and the full-density shield in the main report.

References

Sources

  1. 1.Stewart-Jones GBE, et al. Trimeric HIV-1-Env structures define glycan shields from clades A, B, and G. Cell 2016;165:813–826. doi:10.1016/j.cell.2016.04.010. PDB 5FYJ (clade G X1193.c1 SOSIP.664 with PGT122, 35O22 and VRC01).
  2. 2.Tsai YX, et al. Rapid simulation of glycoprotein structures by grafting and steric exclusion of glycan conformer libraries (GlycoSHIELD). Cell 2024;187:1296–1311. doi:10.1016/j.cell.2024.01.034
  3. 3.Tsai YX, et al. GlycoSHIELD glycan conformer library, version 6.0 (file gs.27.M.Man9.tar.gz used). Zenodo 2023. doi:10.5281/zenodo.8422323 (concept record doi:10.5281/zenodo.8414255).
  4. 4.Briggs JAG, et al. Structural organization of authentic, mature HIV-1 virions and cores. EMBO J 2003;22:1707–1715. doi:10.1093/emboj/cdg143
  5. 5.Zhu P, et al. Distribution and three-dimensional structure of AIDS virus envelope spikes. Nature 2006;441:847–852. doi:10.1038/nature04817
  6. 6.Mattei S, et al. The structure and flexibility of conical HIV-1 capsids determined within intact virions. Science 2016;354:1434–1437. doi:10.1126/science.aah4972
  7. 7.Saphire EO, et al. Crystal structure of a neutralizing human IgG against HIV-1: a template for vaccine design. Science 2001;293:1155–1159. doi:10.1126/science.1061692. PDB 1HZH.
  8. 8.Walker LM, et al. Broad neutralization coverage of HIV by multiple highly potent antibodies (PGT121, PGT122, PGT128). Nature 2011;477:466–470. doi:10.1038/nature10373
  9. 9.Huang J, et al. Broad and potent HIV-1 neutralization by a human antibody that binds the gp41–gp120 interface (35O22). Nature 2014;515:138–142. doi:10.1038/nature13601
  10. 10.Zhou T, et al. Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01. Science 2010;329:811–817. doi:10.1126/science.1192819. PDB 3NGB.