ArticleBiochemistry2017
Structural Analysis of the Glycosylated Intact HIV-1 gp120-b12 Antibody Complex Using Hydroxyl Radical Protein Footprinting.
Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 33 citations in OpenAlex.
- Recommendations and considerations for hydroxyl radical protein footprinting-mass spectrometry.Nature methods · 2026Review
- Multidose Inline Size-Exclusion Chromatography-Flash Oxidation for Structural Analysis of Dynamic Protein-Ligand Interactions of Antithrombin III and Unfractionated Heparin.Analytical chemistry · 2026Article
- Radical footprinting in mammalian whole blood.Nature communications · 2026Article
- Towards Understanding the Basis of Brucella Antigen-Antibody Specificity.Molecules (Basel, Switzerland) · 2025Article
- Residue-Specific Epitope Mapping of the PD-1/Nivolumab Interaction Using X-ray Footprinting Mass Spectrometry.Antibodies (Basel, Switzerland) · 2024Article
- Structural Investigation of Therapeutic Antibodies Using Hydroxyl Radical Protein Footprinting Methods.Antibodies (Basel, Switzerland) · 2022Review
- IgG1-b12-HIV-gp120 Interface in Solution: A Computational Study.Journal of chemical information and modeling · 2022Article
- Inline Liquid Chromatography-Fast Photochemical Oxidation of Proteins for Targeted Structural Analysis of Conformationally Heterogeneous Mixtures.Analytical chemistry · 2021Article
- Enabling Real-Time Compensation in Fast Photochemical Oxidations of Proteins for the Determination of Protein Topography Changes.Journal of visualized experiments : JoVE · 2020Article
- Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications.Chemical reviews · 2020Review
- Rapid Quantification of Peptide Oxidation Isomers From Complex Mixtures.Analytical chemistry · 2020Article
- Composite Conformational Changes of Signaling Proteins upon Ligand Binding Revealed by a Single Approach: Calcium-Calmodulin Study.Analytical chemistry · 2019Article
- Predicting Protein Complex Structure from Surface-Induced Dissociation Mass Spectrometry Data.ACS central science · 2019Article
- Glycosylation influences activity, stability and immobilization of the feruloyl esterase 1a from Myceliophthora thermophila.AMB Express · 2019Article
- Fast photochemical oxidation of proteins (FPOP): A powerful mass spectrometry-based structural proteomics tool.The Journal of biological chemistry · 2019Review
- Illuminating Biological Interactions with in Vivo Protein Footprinting.Analytical chemistry · 2019Article
- Predicting the Structures of Glycans, Glycoproteins, and Their Complexes.Chemical reviews · 2018Review
- Variation in FPOP Measurements Is Primarily Caused by Poor Peptide Signal Intensity.Journal of the American Society for Mass Spectrometry · 2018Article
- All-atom virus simulations.Current opinion in virology · 2018Review
- Modifications generated by fast photochemical oxidation of proteins reflect the native conformations of proteins.Protein science : a publication of the Protein Society · 2018Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
Abstract
Glycoprotein gp120 is a surface antigen and virulence factor of human immunodeficiency virus 1. Broadly neutralizing antibodies (bNAbs) that react to gp120 from a variety of HIV isolates offer hope for the development of broadly effective immunogens for vaccination purposes, if the interactions between gp120 and bNAbs can be understood. From a structural perspective, gp120 is a particularly difficult system because of its size, the presence of multiple flexible regions, and the large amount of glycosylation, all of which are important in gp120-bNAb interactions. Here, the interaction of full-length, glycosylated gp120 with bNAb b12 is probed using high-resolution hydroxyl radical protein footprinting (HR-HRPF) by fast photochemical oxidation of proteins. HR-HRPF allows for the measurement of changes in the average solvent accessible surface area of multiple amino acids without the need for measures that might alter the protein conformation, such as mutagenesis. HR-HRPF of the gp120-b12 complex coupled with computational modeling shows a novel extensive interaction of the V1/V2 domain, probably with the light chain of b12. Our data also reveal HR-HRPF protection in the C3 domain caused by interaction of the N330 glycan with the b12 light chain. In addition to providing information about the interactions of full-length, glycosylated gp120 with b12, this work serves as a template for the structural interrogation of full-length glycosylated gp120 with other bNAbs to better characterize the interactions that drive the broad specificity of the bNAb.
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