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Glycobiology, Vol 9, 833-839, Copyright © 1999 by Oxford University Press

ORIGINAL ARTICLES

Vesicular-integral membrane protein, VIP36, recognizes high-mannose type glycans containing alpha1-->2 mannosyl residues in MDCK cells

S Hara-Kuge, T Ohkura, A Seko and K Yamashita
Department of Biochemistry, Sasaki Institute, 2-2 Kanda-Surugadai, Chiyoda-ku, Tokyo 101-0062, Japan.

The 36 kDa vesicular-integral membrane protein, VIP36, has been originally isolated from MDCK cells as a component of glycolipid- enriched detergent-insoluble complexes containing apical marker proteins, and its luminal domain shows homology to leguminous plant lectins and ERGIC-53. As the first step to identify the functional role of VIP36, the carbohydrate binding specificity of VIP36 was investigated using a fusion protein of glutathione- S -transferase and luminal domain of VIP36 (Vip36). It was found that VIP36 recognizes high-mannose type glycans containing alpha1-->2 Man residues and alpha- amino substituted asparagine. The binding of Vip36 to high-mannose type glycans was independent of Ca(2+)and theoptimal condition was pH 6.0 at 37 degrees C. The concentration at which half inhibition of the binding by Man(7-9).GlcNAc(2). N Ac. Asn occurred was 1.0 x 10(-9)M. The association constant between Man(7-9).GlcNAc(2)in porcine thyroglobulin and immobilized Vip36 was 2.1 x 10(8)M(-1)as determined by means of a biosensor based on surface plasmon resonance. These results indicate that VIP36 functions as an intracellular lectin recognizing glycoproteins which possess high-mannose type glycans, (Manalpha1-- >2)(2-4).Man(5). GlcNAc(2).
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