ArticleBioconjugate chemistry2021
Efficient Labeling of Native Human IgG by Proximity-Based Sortase-Mediated Isopeptide Ligation.
Article in Bioconjugate chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- The evolving landscape of enzymatic technologies for precision synthesis of antibody-drug conjugates.Antibody therapeutics · 2026Review
- Phage-Selected Clickable Gln-Donor Peptide for Lys-Selective Fab Labeling Using Engineered Microbial Transglutaminase.Antibodies (Basel, Switzerland) · 2026Article
- Tools For Building Artificial Biological Nanostructures.ACS nano · 2026Review
- Structural and functional evolution of IL-1 targeting: From systemic neutralization to bioengineered nanotherapies.Materials today. Bio · 2026Review
- Site-specific labelling of native peptides and proteins: chemical and enzymatic strategies.Beilstein journal of organic chemistry · 2026Review
- A Putative Interaction between the Transmembrane Domains ofThe journal of physical chemistry. B · 2025Article
- Development of a Versatile Cancer Vaccine Format Targeting Antigen-Presenting Cells Using Proximity-Based Sortase A-Mediated Ligation of T-Cell Epitopes.Bioconjugate chemistry · 2024Article
- Sortase-mediated labeling: Expanding frontiers in site-specific protein functionalization opens new research avenues.Current opinion in chemical biology · 2024Review
- Sortase mediated protein ubiquitination with defined chain length and topology.RSC chemical biology · 2024Article
- Bicyclic Engineered Sortase A Performs Transpeptidation under Denaturing Conditions.Bioconjugate chemistry · 2023Article
- Precision Modification of Native Antibodies.Bioconjugate chemistry · 2021Review
- Affinity-Based Methods for Site-Specific Conjugation of Antibodies.Bioconjugate chemistry · 2021Review
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
Antibody-drug conjugates (ADCs) have demonstrated great therapeutic potential due to their ability to target the delivery of potent cytotoxins. However, the heterogeneous nature of conventional drug conjugation strategies can affect the safety, efficacy, and stability of ADCs. Site-specific conjugations can resolve these issues, but often require genetic modification of Immunoglobulin G (IgG), which can impact yield or cost of production, or require undesirable chemical linkages. Here, we describe a near-traceless conjugation method that enables the efficient modification of native IgG, without the need for genetic engineering or glycan modification. This method utilizes engineered variants of sortase A to catalyze noncanonical isopeptide ligation. Sortase A was fused to an antibody-binding domain to improve ligation efficiency. Antibody labeling is limited to five lysine residues on the heavy chain and one on the light chain of human IgG1. The ADCs exhibit conserved antigen and Fc-receptor interactions, as well as potent cytolytic activity.
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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 OpenQuestion graph.