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TitleCo-evolution of HIV Envelope and Apex-Targeting Neutralizing Antibody Lineage Provides Benchmarks for Vaccine Design.
Journal, issue, pagesCell Rep, Vol. 23, Issue 11, Page 3249-3261, Year 2018
Publish dateJun 12, 2018
AuthorsKimmo Rantalainen / Zachary T Berndsen / Sasha Murrell / Liwei Cao / Oluwarotimi Omorodion / Jonathan L Torres / Mengyu Wu / Jeffrey Umotoy / Jeffrey Copps / Pascal Poignard / Elise Landais / James C Paulson / Ian A Wilson / Andrew B Ward /
PubMed AbstractBroadly neutralizing antibodies (bnAbs) targeting the HIV envelope glycoprotein (Env) typically take years to develop. Longitudinal analyses of both neutralizing antibody lineages and viruses at ...Broadly neutralizing antibodies (bnAbs) targeting the HIV envelope glycoprotein (Env) typically take years to develop. Longitudinal analyses of both neutralizing antibody lineages and viruses at serial time points during infection provide a basis for understanding the co-evolutionary contest between HIV and the humoral immune system. Here, we describe the structural characterization of an apex-targeting antibody lineage and autologous clade A viral Env from a donor in the Protocol C cohort. Comparison of Ab-Env complexes at early and late time points reveals that, within the antibody lineage, the CDRH3 loop rigidifies, the bnAb angle of approach steepens, and surface charges are mutated to accommodate glycan changes. Additionally, we observed differences in site-specific glycosylation between soluble and full-length Env constructs, which may be important for tuning optimal immunogenicity in soluble Env trimers. These studies therefore provide important guideposts for design of immunogens that prime and mature nAb responses to the Env V2-apex.
External linksCell Rep / PubMed:29898396 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.643 - 30.0 Å
Structure data

7858

6dcq

EMDB-7858, PDB-6dcq:
Ectodomain of full length, wild type HIV-1 glycoprotein clone PC64M18C043 in complex with PGT151 Fab
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-7859:
Full Length HIV-1 Envelope Glycoprotein clone PC64M18C043 in complex with PGT151 Fab and PCT64-35S Fab
Method: EM (single particle) / Resolution: 6.8 Å

EMDB-7860:
HIV-1 Envelope Glycoprotein clone PC64M18C043.SOSIP.664 complex with PGT151 Fab
Method: EM (single particle) / Resolution: 4.9 Å

EMDB-7861:
Full length HIV-1 Envelope Glycoprotein clone PC64M4C054 in complex with PGT151 Fab and PCT64-13C Fab
Method: EM (single particle) / Resolution: 30.0 Å

EMDB-7862:
HIV-1 Envelope Glycoprotein clone PC64M4C054.SOSIP.664 in complex with PCT64-13F Fab
Method: EM (single particle) / Resolution: 30.0 Å

EMDB-7863:
HIV-1 Envelope Glycoprotein clone PC64M4C054.SOSIP.664 in complex with PCT64_13C Fab
Method: EM (single particle) / Resolution: 5.1 Å

EMDB-7864:
HIV-1 Envelope Glycoprotein clone PC64M4C054.SOSIP.664.N130A in complex with PCT64_13C Fab
Method: EM (single particle) / Resolution: 30.0 Å

EMDB-7865:
HIV-1 Envelope Glycoprotein clone PC64M4C054.SOSIP in complex with PCT64-35S Fab
Method: EM (single particle) / Resolution: 5.5 Å

EMDB-7866:
HIV-1 Envelope Glycoprotein clone PC64M4C054.SOSIP.664.N130A in complex with PCT64_35S Fab
Method: EM (single particle) / Resolution: 8.2 Å

PDB-6ca6:
Crystal structure of PCT64_35S, a broadly neutralizing anti-HIV antibody.
Method: X-RAY DIFFRACTION / Resolution: 2.43 Å

PDB-6ca7:
Crystal structure of PCT64_13C, a strain specific anti-HIV antibody
Method: X-RAY DIFFRACTION / Resolution: 1.643 Å

PDB-6ca9:
Crystal structure of Fab PCT64_LMCA (SAR), the least mutated common ancestor of the HIV-1 broadly neutralizing antibody lineage PCT64
Method: X-RAY DIFFRACTION / Resolution: 2.702 Å

Chemicals

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • homo sapiens (human)
  • human immunodeficiency virus 1
KeywordsIMMUNE SYSTEM / Antibody / neutralizing / IgG1 / HIV-1 / bNAb / VIRAL PROTEIN / Glycoprotein / Env

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