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Ludwig, Anna-Kristin; Kaltner, Herbert; Kopitz, Jürgen and Gabius, Hans-Joachim (2019): Lectinology 4.0: Altering modular (ga)lectin display for functional analysis and biomedical applications. In: Biochimica et Biophysica Acta-General Subjects, Vol. 1863, No. 5: pp. 935-940

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Background: Recognition of glycans by lectins is emerging as (patho)physiologically broadly used mode of cellular information transfer. Whereas the direct ligand-receptor contact is often already thoroughly characterized, the functional relevance of aspects of architecture such as modular design and valence of lectins is less well defined. Scope of review: Following an introduction to modular lectin design, three levels of methodology are then reviewed that delineate lectin structure-activity relationships beyond glycan binding, with emphasis on domain shuffling. Major conclusions: Engineering of variants by modular transplantation facilitates versatile Nature-inspired design switches and access to new combinations with translational potential, as exemplified for human adhesion/growth-regulatory galectins. General significance: To gain an understanding of the functional significance of natural variations in quaternary structure and modular design within a protein family is a current challenge. Strategic application of methods of the described phases is a means to respond to this challenge.

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