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Parameters and determinants of responses to selection in antibody libraries

Steven Schulz, Sébastien Boyer, Matteo Smerlak, Simona Cocco, Rémi Monasson, Clément Nizak, Olivier Rivoire
doi: https://doi.org/10.1101/712539
Steven Schulz
aCenter for Interdisciplinary Research in Biology (CIRB), Collège de France, CNRS UMR 7241, INSERM U1050, PSL University, Paris, France
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Sébastien Boyer
bDépartement de biochimie, Faculté de Médecine, Université de Montréal, Montréal, Canada
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Matteo Smerlak
cMax Planck Institute for Mathematics in the Sciences, Leipzig, Germany
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Simona Cocco
dLaboratory of Physics of École Normale Supérieure, UMR 8023, CNRS & PSL University, Paris, France
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Rémi Monasson
dLaboratory of Physics of École Normale Supérieure, UMR 8023, CNRS & PSL University, Paris, France
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Clément Nizak
eChimie Biologie Innovation, ESPCI Paris, CNRS, PSL University, Paris, France
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Olivier Rivoire
aCenter for Interdisciplinary Research in Biology (CIRB), Collège de France, CNRS UMR 7241, INSERM U1050, PSL University, Paris, France
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  • For correspondence: olivier.rivoire@college-de-france.fr
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Abstract

Antibody repertoires contain binders to nearly any target antigen. The sequences of these antibodies differ mostly at few sites located on the surface of a scaffold that itself consists of much less varied amino acids. What is the impact of this scaffold on the response to selection of a repertoire? To gauge this impact, we carried out quantitative phage display experiments with three antibody libraries based on distinct scaffolds harboring the same diversity at randomized sites, which we selected for binding to four arbitrary targets. We first show that the response to selection of an antibody library is captured by a simple and measurable parameter with direct physical and information-theoretic interpretations. Second, we identify a major determinant of this parameter which is encoded in the scaffold, its degree of evolutionary maturation. Antibodies undergo an accelerated evolutionary process, called affinity maturation, to improve their affinity to a given target antigen as part of the adaptive immune response. We find that libraries of antibodies built around such maturated scaffolds have a lower response to selection to other arbitrary targets than libraries built around naïve scaffolds of germline origin. Our results are a first step towards quantifying and controlling the evolutionary potential of biomolecules.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted July 23, 2019.
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Parameters and determinants of responses to selection in antibody libraries
Steven Schulz, Sébastien Boyer, Matteo Smerlak, Simona Cocco, Rémi Monasson, Clément Nizak, Olivier Rivoire
bioRxiv 712539; doi: https://doi.org/10.1101/712539
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Parameters and determinants of responses to selection in antibody libraries
Steven Schulz, Sébastien Boyer, Matteo Smerlak, Simona Cocco, Rémi Monasson, Clément Nizak, Olivier Rivoire
bioRxiv 712539; doi: https://doi.org/10.1101/712539

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