Skip Navigation



Journal of Biochemistry Advance Access published online on January 18, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm043
This Article
Right arrow Advance Access manuscript (PDF)
Right arrow All Versions of this Article:
141/3/389    most recent
mvm043v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Yabe, R.
Right arrow Articles by Hirabayashi, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yabe, R.
Right arrow Articles by Hirabayashi, J.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 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, 3Department of Biochemistry, National Institute of Agrobiological Sciences, Tsukuba, Ibaraki 305-8602, Japan

*Corresponding author: Atsushi Kuno, Glycostructure Analysis Team, Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba Central 2, 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568, Japan. Phone: +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


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J BiochemHome page
H. Kaku, H. Kaneko, N. Minamihara, K. Iwata, E. T. Jordan, M. A. Rojo, N. Minami-Ishii, E. Minami, S. Hisajima, and N. Shibuya
Elderberry Bark Lectins Evolved to Recognize Neu5Ac{alpha}2,6Gal/GalNAc Sequence from a Gal/GalNAc Binding Lectin Through the Substitution of Amino-Acid Residues Critical for the Binding to Sialic Acid
J. Biochem., September 1, 2007; 142(3): 393 - 401.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.