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J. Biol. Chem., Vol. 278, Issue 34, 32439-32447, August 22, 2003

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A New Fungal Lectin Recognizing (1–6)-linked Fucose in the N-Glycan^*

Yasuo Oda , Tsutomu Senaha, Yuuki Matsuno, Kazuki Nakajima, Ryousuke Naka, Mitsuhiro Kinoshita, Eiko Honda , Itaru Furuta  and Kazuaki Kakehi

From the Faculty of Pharmaceutical Sciences, Kinki University, Kowakae 3-4-1, Higashi-Osaka, Japan 577-8502 and the Life Science Research Institute, Kinki University, Ohono-Higashi 377-2, Osaka-Sayama, Japan 589-8511

In this report, we describe a new lectin from the fungus Rhizopus stolonifer that agglutinates rabbit red blood cells. Agglutinating activity was detected in the extract of mycelium-forming spores cultured on agar plates but not in the mycelium-forming no spores from liquid medium. This lectin, which we designated R. stolonifer lectin (RSL), was isolated by affinity chromatography with porcine stomach mucin-Sepharose. SDS-polyacrylamide gel electrophoresis and mass spectral analysis showed that RSL is 4.5 kDa, whereas gel filtration indicated a mass of 28 kDa. This indicates that the lectin is a hexamer of noncovalently associated RSL monomers. RSL activity was very stable, since it was insensitive to heat treatment at 70 °C for 10 min. Analysis of RSL binding specificity by both microtiter plate and precipitation assays showed that N-glycans with L-fucose linked to the reducing terminal GlcNAc residues are the most potent inhibitors of RSL binding, whereas N-glycans without (1–6)-linked fucose residues are 100-fold weaker inhibitors of binding. Oligosaccharides with (1–2, –3, and –4) linkages showed no inhibition of binding in these assays. In a mirror resonance biosensor assay, high affinity binding was observed between RSL and the glycopeptide of bovine -globulin, which has N-glycans with (1–6)-linked fucose residues. However, RSL showed only a weak interaction with the glycopeptide of quail ovomucoid, which lacks fucose residues. Finally, capillary affinity electrophoresis studies indicated that RSL binds strongly to N-glycans with (1–6)-linked fucose residues. Together, these results show that RSL recognizes the core structure of N-glycans with (1–6)-linked L-fucose residues. This specificity could make RSL a valuable tool for glycobiological studies.

Received for publication, May 16, 2003 , and in revised form, June 4, 2003.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Faculty of Pharmaceutical Sciences, Kinki University, Kowakae 3-4-1, Higashi-Osaka, Japan 577-8502. Tel.: 81-6-6721-2332 (ext. 3829); Fax: 81-6-6730-1394; E-mail: y_oda{at}phar.kindai.ac.jp.

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