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Journal of Biochemistry Advance Access originally published online on January 18, 2007
Journal of Biochemistry 2007 141(3):389-399; doi:10.1093/jb/mvm043
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© 2007 The Japanese Biochemical Society.

Tailoring a Novel Sialic Acid-Binding Lectin from a Ricin-B Chain-like Galactose-Binding Protein by Natural Evolution-Mimicry

Rikio Yabe1,2, Ryuichiro Suzuki1, Atsushi Kuno1,*, Zui Fujimoto3, Yoshifumi Jigami1,2 and Jun Hirabayashi1

1Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki 305-8568, Japan; 2Graduate School of Life and Environmental Sciences, University of Tsukuba, Tsukuba, Ibaraki 305-8572, Japan; and 3Department of Biochemistry, National Institute of Agrobiological Sciences, Tsukuba, Ibaraki 305-8602, Japan

*To whom correspondence should be addressed. Tel: +81-29-861-3187, Fax: +81-29-861-3125, E-mail: atsu-kuno{at}aist.go.jp

Received December 2, 2006; Accepted January 6, 2007


  Abstract

Sialic acid (Sia) is a typical terminal sugar, which modifies various types of glycoconjugates commonly found in higher animals. Its regulatory roles in diverse biological phenomena are frequently triggered by interaction with Sia-binding lectins. When using natural Sia-binding lectins as probes, however, there have been practical problems concerning their repertoire and availability. Here, we show a rational creation of a Sia-binding lectin based on the strategy ‘natural evolution-mimicry’, where Sia-binding lectins are engineered by error-prone PCR from a Gal-binding lectin used as a scaffold protein. After selection with fetuin–agarose using a recently reinforced ribosome display system, one of the evolved mutants SRC showed substantial affinity for {alpha}2-6Sia, which the parental Gal-binding lectin EW29Ch lacked. SRC was found to have additional practical advantages in productivity and in preservation of affinity for Gal. Thus, the developed novel Sia-recognition protein will contribute as useful tools to sialoglycomics.

Key Words: glycomics, natural evolution, ribosome display, ricin-B chain, Sia-binding lectin

Abbreviations: EW29, earthworm 29-kDa lectin; EW29Ch, C-terminal domain of EW29; EW29Nh, N-terminal domain of EW29; FAC, frontal affinity chromatography; PA, pyridylaminated; pNP, p-nitrophenyl; SRC, Sia-recognition EW29Ch


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