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| Title | Model Building and Refinement of a Natively Glycosylated HIV-1 Env Protein by High-Resolution Cryoelectron Microscopy. |
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| Journal, issue, pages | Structure, Vol. 23, Issue 10, Page 1943-1951, Year 2015 |
| Publish date | Oct 6, 2015 |
 Authors | Jeong Hyun Lee / Natalia de Val / Dmitry Lyumkis / Andrew B Ward /  |
| PubMed Abstract | Secretory and membrane proteins from mammalian cells undergo post-translational modifications, including N-linked glycosylation, which can result in a large number of possible glycoforms. This sample ...Secretory and membrane proteins from mammalian cells undergo post-translational modifications, including N-linked glycosylation, which can result in a large number of possible glycoforms. This sample heterogeneity can be problematic for structural studies, particularly X-ray crystallography. Thus, crystal structures of heavily glycosylated proteins such as the HIV-1 Env viral spike protein have been determined by removing the majority of glycans. This step is most frequently carried out using Endoglycosidase H (EndoH) and requires that all expressed glycans be in the high-mannose form, which is often not the native glycoform. With significantly improved technologies in single-particle cryoelectron microscopy, we demonstrate that it is now possible to refine and build natively glycosylated HIV-1 Env structures in solution to 4.36 Å resolution. At this resolution we can now analyze the complete epitope of a broadly neutralizing antibody (bnAb), PGT128, in the context of the trimer expressed with native glycans. |
 External links | Structure / PubMed:26388028 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 4.36 - 4.47 Å |
| Structure data |  EMDB-3120: |
| Chemicals |  ChemComp-NAG: |
| Source |
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 Keywords | VIRAL PROTEIN / IMMUNE SYSTEM / HIV-1 / ENV / BNAB / ANTIBODY / PGT128 |
human immunodeficiency virus 1
homo sapiens (human)