|Entry||Database: EMDB / ID: 8168|
|Title||BF520.1 Fab fragment bound to BG505 T332N SOSIP.664 trimer|
|Map data||BF520.1 Fab fragment bound to BG505 T332N SOSIP.664 trimer|
|Sample||BF520.1 Fab complexed with BG505.C2 T332N SOSIP.664 trimer:|
BF520.1 Fab / BG505.C2 T332N SOSIP.664 trimer
|Source||Homo sapiens (human) / Human immunodeficiency virus 1|
|Method||single particle reconstruction / 10.9 Å resolution|
|Authors||Williams JA / Lee KK|
|Citation||Journal: Cell / Year: 2016|
Title: HIV-1 Neutralizing Antibodies with Limited Hypermutation from an Infant.
Authors: Cassandra A Simonich / Katherine L Williams / Hans P Verkerke / James A Williams / Ruth Nduati / Kelly K Lee / Julie Overbaugh
Abstract: HIV-1 broadly neutralizing antibodies (bnAbs) develop in a subset of infected adults and exhibit high levels of somatic hypermutation (SHM) due to years of affinity maturation. There is no precedent ...HIV-1 broadly neutralizing antibodies (bnAbs) develop in a subset of infected adults and exhibit high levels of somatic hypermutation (SHM) due to years of affinity maturation. There is no precedent for eliciting highly mutated antibodies by vaccination, nor is it practical to wait years for a desired response. Infants develop broad responses early, which may suggest a more direct path to generating bnAbs. Here, we isolated ten neutralizing antibodies (nAbs) contributing to plasma breadth of an infant at ∼1 year post-infection, including one with cross-clade breadth. The nAbs bind to envelope trimer from the transmitted virus, suggesting that this interaction may have initiated development of the infant nAbs. The infant cross-clade bnAb targets the N332 supersite on envelope but, unlike adult bnAbs targeting this site, lacks indels and has low SHM. The identification of this infant bnAb illustrates that HIV-1-specific neutralization breadth can develop without prolonged affinity maturation and extensive SHM.
|Date||Deposition: Apr 29, 2016 / Header (metadata) release: Jul 13, 2016 / Map release: Jul 13, 2016 / Last update: Feb 14, 2018|
|Structure viewer||EM map: |
Downloads & links
|File||emd_8168.map.gz (map file in CCP4 format, 2371 KB)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 4.14 Å|
CCP4 map header:
-Entire BF520.1 Fab complexed with BG505.C2 T332N SOSIP.664 trimer
|Entire||Name: BF520.1 Fab complexed with BG505.C2 T332N SOSIP.664 trimer|
Number of components: 3
-Component #1: protein, BF520.1 Fab complexed with BG505.C2 T332N SOSIP.664 trimer
|Protein||Name: BF520.1 Fab complexed with BG505.C2 T332N SOSIP.664 trimer|
Recombinant expression: No
-Component #2: protein, BF520.1 Fab
|Protein||Name: BF520.1 Fab|
Details: Fab domains generated by papain digestion of BF520.1 IgG
Recombinant expression: No
|Source||Species: Homo sapiens (human)|
-Component #3: protein, BG505.C2 T332N SOSIP.664 trimer
|Protein||Name: BG505.C2 T332N SOSIP.664 trimer / Recombinant expression: No|
|Source||Species: Human immunodeficiency virus 1 / Strain: BG505.C2 T332N|
|Source (engineered)||Expression System: Homo sapiens (human) / Vector: pPPI4 / Cell of expression system: HEK 293F|
|Specimen||Specimen state: particle|
|Sample solution||Specimen conc.: 0.02 mg/ml / pH: 7.5|
|Vitrification||Cryogen name: NONE|
-Electron microscopy imaging
Model: Tecnai Spirit / Image courtesy: FEI Company
|Imaging||Microscope: FEI TECNAI SPIRIT|
|Electron gun||Electron source: LAB6 / Accelerating voltage: 120 kV / Electron dose: 24 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Magnification: 52000.0 X (nominal) / Imaging mode: BRIGHT FIELD / Defocus: 500.0 - 3000.0 nm|
|Specimen Holder||Model: SIDE ENTRY, EUCENTRIC|
|Camera||Detector: GATAN ULTRASCAN 4000 (4k x 4k)|
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