ArticleThe Journal of biological chemistry2017
A Monoclonal Antibody to Cryptococcus neoformans Glucuronoxylomannan Manifests Hydrolytic Activity for Both Peptides and Polysaccharides.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers, 1 of them a synthesis that pooled it.
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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
33 citing papers in PubMed, 1 synthesis or guideline pooled it, 52 citations in OpenAlex.
- Immunoglobulins with Non-Canonical Functions in Inflammatory and Autoimmune Disease States.International journal of molecular sciences · 2020Pooled it
- Unexpected Variability in Laboratory and Clinical Assays Used to Quantify Cryptococcus neoformans Polysaccharide.The Journal of infectious diseases · 2026Article
- Effects of human immunoglobulins onmBio · 2026Article
- Immune evasion, dysregulation, and emerging immunotherapies for invasive fungal infections in the immunocompromised host.Frontiers in immunology · 2026Review
- Article
- Monoclonal Antibody Therapies for Infectious Diseases.Current topics in microbiology and immunology · 2025Review
- Monoclonal antibodies: From magic bullet to precision weapon.Molecular biomedicine · 2024Review
- Immunoglobulin constant regions provide stabilization to the paratope and enforce epitope specificity.The Journal of biological chemistry · 2024Article
- Enzymatization of mouse monoclonal antibodies to the corresponding catalytic antibodies.Scientific reports · 2024Article
- Catalytic Protein Inhibitors.Angewandte Chemie (International ed. in English) · 2024Review
- Cryptococcosis and Cryptococcal Meningitis: A Narrative Review and the Up-to-Date Management Approach.Cureus · 2024Review
- Neutron Scattering Analysis ofBiomacromolecules · 2024Article
- Intracellular Pathogens: Infection, Immunity, and Intervention.Methods in molecular biology (Clifton, N.J.) · 2024Review
- Methods of Cryptococcal Polysaccharide Analysis Using ELISA.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Neutron Scattering Analysis ofbioRxiv : the preprint server for biology · 2023Article
- Catalytic spike antibodies: A new paradigm in neutralization.Cell chemical biology · 2023Article
- Direct conversion of a general antibody to its catalytic antibody and corresponding applications -Importance and role of Pro95 in CDR-3.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2023Review
- Obtaining Highly Active Catalytic Antibodies Capable of Enzymatically Cleaving Antigens.International journal of molecular sciences · 2022Article
- A new catalytic site functioning in antigen cleavage by H34 catalytic antibody light chain.Scientific reports · 2022Article
- Experimental Autoimmune Encephalomyelitis of Mice: Enzymatic Cross Site-Specific Hydrolysis of H4 Histone by IgGs against Histones and Myelin Basic Protein.International journal of molecular sciences · 2022Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Studies in the 1980s first showed that some natural antibodies were "catalytic" and able to hydrolyze peptide or phosphodiester bonds in antigens. Many naturally occurring catalytic antibodies have since been isolated from human sera and associated with positive and negative outcomes in autoimmune disease and infection. The function and prevalence of these antibodies, however, remain unclear. A previous study suggested that the 18B7 monoclonal antibody against glucuronoxylomannan (GXM), the major component of the Cryptococcus neoformans polysaccharide capsule, hydrolyzed a peptide antigen mimetic. Using mass spectrometry and Förster resonance energy transfer techniques, we confirm and characterize the hydrolytic activity of 18B7 against peptide mimetics and show that 18B7 is able to hydrolyze an oligosaccharide substrate, providing the first example of a naturally occurring catalytic antibody for polysaccharides. Additionally, we show that the catalytic 18B7 antibody increases release of capsular polysaccharide from fungal cells. A serine protease inhibitor blocked peptide and oligosaccharide hydrolysis by 18B7, and a putative serine protease-like active site was identified in the light chain variable region of the antibody. An algorithm was developed to detect similar sites present in unique antibody structures in the Protein Data Bank. The putative site was found in 14 of 63 (22.2%) catalytic antibody structures and 119 of 1602 (7.4%) antibodies with no annotation of catalytic activity. The ability of many antibodies to cleave antigen, albeit slowly, supports the notion that this activity is an important immunoglobulin function in host defense. The discovery of GXM hydrolytic activity suggests new therapeutic possibilities for polysaccharide-binding antibodies.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.