IgGs are made for walking on bacterial and viral surfaces View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2014-12

AUTHORS

Johannes Preiner, Noriyuki Kodera, Jilin Tang, Andreas Ebner, Mario Brameshuber, Dieter Blaas, Nicola Gelbmann, Hermann J. Gruber, Toshio Ando, Peter Hinterdorfer

ABSTRACT

Binding of antibodies to their cognate antigens is fundamental for adaptive immunity. Molecular engineering of antibodies for therapeutic and diagnostic purposes emerges to be one of the major technologies in combating many human diseases. Despite its importance, a detailed description of the nanomechanical process of antibody-antigen binding and dissociation on the molecular level is lacking. Here we utilize high-speed atomic force microscopy to examine the dynamics of antibody recognition and uncover a principle; antibodies do not remain stationary on surfaces of regularly spaced epitopes; they rather exhibit 'bipedal' stochastic walking. As monovalent Fab fragments do not move, steric strain is identified as the origin of short-lived bivalent binding. Walking antibodies gather in transient clusters that might serve as docking sites for the complement system and/or phagocytes. Our findings could inspire the rational design of antibodies and multivalent receptors to exploit/inhibit steric strain-induced dynamic effects. More... »

PAGES

4394

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ncomms5394

DOI

http://dx.doi.org/10.1038/ncomms5394

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1039294503

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/25008037


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