ArticleActa crystallographica. Section D, Biological crystallography2008
Structure determination of an anti-HIV-1 Fab 447-52D-peptide complex from an epitaxially twinned data set.
Article in Acta crystallographica. Section D, Biological crystallography, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 32 citations in OpenAlex.
- Crystal structures of the human IgD Fab reveal insights into CMolecular immunology · 2023Article
- Characterizing pathological imperfections in macromolecular crystals: lattice disorders and modulations.Crystallography reviews · 2020Article
- Difficult-to-neutralize global HIV-1 isolates are neutralized by antibodies targeting open envelope conformations.Nature communications · 2019Article
- Computational-guided determination of the functional role of 447-52D long CDRH3.Protein engineering, design & selection : PEDS · 2018Article
- HIV-1 gp41 Residues Modulate CD4-Induced Conformational Changes in the Envelope Glycoprotein and Evolution of a Relaxed Conformation of gp120.Journal of virology · 2018Article
- Increased Epitope Complexity Correlated with Antibody Affinity Maturation and a Novel Binding Mode Revealed by Structures of Rabbit Antibodies against the Third Variable Loop (V3) of HIV-1 gp120.Journal of virology · 2018Article
- Article
- Visualization of retroviral envelope spikes in complex with the V3 loop antibody 447-52D on intact viruses by cryo-electron tomography.Journal of virology · 2014Article
- The rotational order-disorder structure of the reversibly photoswitchable red fluorescent protein rsTagRFP.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Computational prediction of neutralization epitopes targeted by human anti-V3 HIV monoclonal antibodies.PloS one · 2014Article
- A mammalian cell based FACS-panning platform for the selection of HIV-1 envelopes for vaccine development.PloS one · 2014Article
- Thermodynamic signatures of the antigen binding site of mAb 447-52D targeting the third variable region of HIV-1 gp120.Biochemistry · 2013Article
- Rabbit anti-HIV-1 monoclonal antibodies raised by immunization can mimic the antigen-binding modes of antibodies derived from HIV-1-infected humans.Journal of virology · 2013Article
- Cross-clade HIV-1 neutralizing antibodies induced with V3-scaffold protein immunogens following priming with gp120 DNA.Journal of virology · 2011Article
- Structure-guided design and immunological characterization of immunogens presenting the HIV-1 gp120 V3 loop on a CTB scaffold.Virology · 2010Article
- Conserved structural elements in the V3 crown of HIV-1 gp120.Nature structural & molecular biology · 2010Article
- Structure-function relationships of HIV-1 envelope sequence-variable regions refocus vaccine design.Nature reviews. Immunology · 2010Review
- An optimally constrained V3 peptide is a better immunogen than its linear homolog or HIV-1 gp120.Virology · 2010Article
- Structural conservation predominates over sequence variability in the crown of HIV type 1's V3 loop.AIDS research and human retroviruses · 2010Article
- Structural basis of the cross-reactivity of genetically related human anti-HIV-1 mAbs: implications for design of V3-based immunogens.Structure (London, England : 1993) · 2009Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Although antibodies against the third variable loop (V3) of the HIV-1 viral envelope glycoprotein are among the first neutralizing antibodies to be detected in infected individuals, they are normally restricted in their specificity. X-ray crystallographic studies of V3-specific antibodies have contributed to a more thorough understanding of recognition of this epitope and of conserved features in the V3 loop that could potentially aid in the design of a multi-component vaccine. The human antibody 447-52D exhibits relatively broad neutralization of primary viral isolates compared with other V3-loop antibodies. A crystal structure of Fab 447-52D in complex with a V3 peptide (UG1033) was determined at 2.1 angstroms resolution. The structure was determined using an epitaxially twinned data set and in-house programs to detect and remove overlapping reflections. Although the processed data have lower than desired completeness and slightly higher than normal R values for the resolution, good-quality electron-density maps were obtained that enabled structure determination. The structure revealed an extended CDR H3 loop that forms a beta-sheet with the peptide, with the predominant contacts being main-chain hydrogen bonds. The V3 peptide and Fab show high structural homology with the previously reported structures of other Fab 447-52D complexes, reinforcing the idea that the V3 loop may adopt a small set of conserved structures, particularly around the crown of the beta-hairpin.
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