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Nat Nanotechnol. 2019 Feb;14(2):184-190. doi: 10.1038/s41565-018-0336-3. Epub 2019 Jan 14.

Binding to nanopatterned antigens is dominated by the spatial tolerance of antibodies.

Author information

1
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
2
Centre for Immune Regulation (CIR), Department of Immunology, Oslo University Hospital, Rikshospitalet, Oslo, Norway.
3
CIR, Department of Biosciences, University of Oslo, Oslo, Norway.
4
Department of Pharmacology, Institute of Clinical Medicine, University of Oslo, Oslo, Norway.
5
Department of Infectious Disease Immunology, Norwegian Institute of Public Health, Oslo, Norway.
6
School of Pharmacy, University of Oslo, Oslo, Norway.
7
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden. bjorn.hogberg@ki.se.

Abstract

Although repetitive patterns of antigens are crucial for certain immune responses, an understanding of how antibodies bind and dynamically interact with various spatial arrangements of molecules is lacking. Hence, we introduced a new method in which molecularly precise nanoscale patterns of antigens are displayed using DNA origami and immobilized in a surface plasmon resonance set-up. Using antibodies with identical antigen-binding domains, we found that all the subclasses and isotypes studied bind bivalently to two antigens separated at distances that range from 3 to 17 nm. The binding affinities of these antibodies change with the antigen distances, with a distinct preference for antigens separated by approximately 16 nm, and considerable differences in spatial tolerance exist between IgM and IgG and between low- and high-affinity antibodies.

Comment in

PMID:
30643273
PMCID:
PMC6420075
DOI:
10.1038/s41565-018-0336-3
[Indexed for MEDLINE]
Free PMC Article

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