期刊
出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.2212658119
关键词
nanobody; glycobiology; immunoglobulin
资金
- Bill and Melinda Gates Foundation [INV-034057]
- National Institute of Allergy and Infectious Diseases [U19AI111825, R01AI155716, R01AI146329, R01AI117927, R01AI137276]
- National Institute of General Medical Sciences [T32GM007739]
- Bill and Melinda Gates Foundation [INV-034057] Funding Source: Bill and Melinda Gates Foundation
This article describes a method to identify and characterize nanobodies that can distinguish specific glycoforms, which is useful for studying protein glycosylation. The method allows for clinical stratification of infected individuals and disruption of specific immune responses.
Protein glycosylation is a crucial mediator of biological functions and is tightly regulated in health and disease. However, interrogating complex protein glycoforms is challenging, as current lectin tools are limited by cross-reactivity while mass spectrometry typically requires biochemical purification and isolation of the target protein. Here, we describe a method to identify and characterize a class of nanobodies that can distinguish glycoforms without reactivity to off-target glycoproteins or glycans. We apply this technology to immunoglobulin G (IgG) Fc glycoforms and define nanobodies that specifically recognize either IgG lacking its core-fucose or IgG bearing terminal sialic acid residues. By adapting these tools to standard biochemical methods, we can clinically stratify dengue virus and SARS-CoV-2 infected individuals based on their IgG glycan profile, selectively disrupt IgG-Fc gamma. receptor binding both in vitro and in vivo, and interrogate the B cell receptor (BCR) glycan structure on living cells. Ultimately, we provide a strategy for the development of reagents to identify and manipulate IgG Fc glycoforms.
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