ArticleThe Journal of biological chemistry2018
Structure-function characterization of three human antibodies targeting the vaccinia virus adhesion molecule D8.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 39 citations in OpenAlex.
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- Monkeypox (Mpox): a comprehensive review of epidemiology, therapeutic advances, and public health implications.Journal of health, population, and nutrition · 2026Review
- Identification of a novel monoclonal antibody derived from the lumpy skin disease virus ORF123 that confers cross-binding and cross-neutralizing activity against Capripoxvirus members.Veterinary research · 2026Article
- Monkey pox (Mpox): pathogenesis, genetic shifts, vaccination strategies and clinical insights.Archives of microbiology · 2026Review
- Broad-Spectrum Antiviral Styrene Maleic-Acid Copolymer Lipid Particle Nanodiscs for pH-Responsive Irreversible Virus Inactivation.Biomacromolecules · 2025Article
- Poxvirus structural biology for application to vaccine design.Trends in immunology · 2025Review
- The evolving mpox threat (2022-2024): clade dynamics, immune evasion, and escalating global health challenges.Frontiers in cellular and infection microbiology · 2025Review
- Identification of mpox M1R and B6R monoclonal and bispecific antibodies that efficiently neutralize authentic mpox virus.Emerging microbes & infections · 2024Article
- Monkeypox virus A29L protein as the target for specific diagnosis and serological analysis.Applied microbiology and biotechnology · 2024Article
- The monkeypox virus-host interplays.Cell insight · 2024Review
- Biological Characteristics and Pathogenesis of Monkeypox Virus: An Overview.Advances in experimental medicine and biology · 2024Review
- Neutralization Determinants on Poxviruses.Viruses · 2023Review
- Generation of recombinant mAbs to vaccinia virus displaying high affinity and potent neutralization.Microbiology spectrum · 2023Article
- Cross-reactive antibody response to Monkeypox virus surface proteins in a small proportion of individuals with and without Chinese smallpox vaccination history.BMC biology · 2023Article
- Human Monkeypox: A Comprehensive Overview of Epidemiology, Pathogenesis, Diagnosis, Treatment, and Prevention Strategies.Pathogens (Basel, Switzerland) · 2023Review
- Functional characterization of hypothetical proteins from Monkeypox virus.Journal, genetic engineering & biotechnology · 2023Article
- Selective events at individual sites underlie the evolution of monkeypox virus clades.Virus evolution · 2023Article
- Functional epitopes and neutralizing antibodies of vaccinia virus.Frontiers in microbiology · 2023Review
- Monkeypox virus emerges from the shadow of its more infamous cousin: family biology matters.Emerging microbes & infections · 2022Review
Corrections and comments
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Authors and funding
18 authors at 6 institutions in 2 countries.
Funding
Abstract
Vaccinia virus (VACV) envelope protein D8 is one of three glycosaminoglycan adhesion molecules and binds to the linear polysaccharide chondroitin sulfate (CS). D8 is also a target for neutralizing antibody responses that are elicited by the smallpox vaccine, which has enabled the first eradication of a human viral pathogen and is a useful model for studying antibody responses. However, to date, VACV epitopes targeted by human antibodies have not been characterized at atomic resolution. Here, we characterized the binding properties of several human anti-D8 antibodies and determined the crystal structures of three VACV-mAb variants, VACV-66, VACV-138, and VACV-304, separately bound to D8. Although all these antibodies bound D8 with high affinity and were moderately neutralizing in the presence of complement, VACV-138 and VACV-304 also fully blocked D8 binding to CS-A, the low affinity ligand for D8. VACV-138 also abrogated D8 binding to the high-affinity ligand CS-E, but we observed residual CS-E binding was observed in the presence of VACV-304. Analysis of the VACV-138- and VACV-304-binding sites along the CS-binding crevice of D8, combined with different efficiencies of blocking D8 adhesion to CS-A and CS-E allowed us to propose that D8 has a high- and low-affinity CS-binding region within its central crevice. The crevice is amenable to protein engineering to further enhance both specificity and affinity of binding to CS-E. Finally, a wild-type D8 tetramer specifically bound to structures within the developing glomeruli of the kidney, which express CS-E. We propose that through structure-based protein engineering, an improved D8 tetramer could be used as a potential diagnostic tool to detect expression of CS-E, which is a possible biomarker for ovarian cancer.
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