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| Title | Differential processing of HIV envelope glycans on the virus and soluble recombinant trimer. |
|---|---|
| Journal, issue, pages | Nat Commun, Vol. 9, Issue 1, Page 3693, Year 2018 |
| Publish date | Sep 12, 2018 |
 Authors | Liwei Cao / Matthias Pauthner / Raiees Andrabi / Kimmo Rantalainen / Zachary Berndsen / Jolene K Diedrich / Sergey Menis / Devin Sok / Raiza Bastidas / Sung-Kyu Robin Park / Claire M Delahunty / Lin He / Javier Guenaga / Richard T Wyatt / William R Schief / Andrew B Ward / John R Yates / Dennis R Burton / James C Paulson /  |
| PubMed Abstract | As the sole target of broadly neutralizing antibodies (bnAbs) to HIV, the envelope glycoprotein (Env) trimer is the focus of vaccination strategies designed to elicit protective bnAbs in humans. ...As the sole target of broadly neutralizing antibodies (bnAbs) to HIV, the envelope glycoprotein (Env) trimer is the focus of vaccination strategies designed to elicit protective bnAbs in humans. Because HIV Env is densely glycosylated with 75-90 N-glycans per trimer, most bnAbs use or accommodate them in their binding epitope, making the glycosylation of recombinant Env a key aspect of HIV vaccine design. Upon analysis of three HIV strains, we here find that site-specific glycosylation of Env from infectious virus closely matches Envs from corresponding recombinant membrane-bound trimers. However, viral Envs differ significantly from recombinant soluble, cleaved (SOSIP) Env trimers, strongly impacting antigenicity. These results provide a benchmark for virus Env glycosylation needed for the design of soluble Env trimers as part of an overall HIV vaccine strategy. |
 External links | Nat Commun / PubMed:30209313 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 4.5 - 6.7 Å |
| Structure data |  EMDB-9030: |
| Chemicals |  ChemComp-NAG: |
| Source |
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 Keywords |  MEMBRANE PROTEIN / Fusion protein-Fab complex |
