✦ LIBER ✦

The specificity of the binding site of AchatininH, a sialic acid-binding lectin from Achatina fulica

✍ Scribed by Goutam Sen; Chitra Mandal

Publisher: Elsevier Science
Year: 1995
Tongue: English
Weight: 671 KB
Volume: 268
Category: Article
ISSN: 0008-6215
DOI: 10.1016/0008-6215(94)00311-3

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✦ Synopsis

A sialic acid-binding lectin, Achatinin n (ATNH) , having unique specificity towards 9-0acetylneuraminic acid, has been purified and characterized. The specificity of this lectin for O-acetylsialic acids was studied in detail, using various sialic acid derivatives and sialoglycoproteins. The potent inhibition of hemagglutination by bovine submaxillary mucin (BSM), which contains 9(7,8)-O-acetylsialic acid and by free 9-O-acetylneuraminic acid confirms the preferential affinity towards this sugar. Further support for the role of O-acetylsialic acid was obtained by sialidase treatment of BSM. O-Deacetylation of the sialic acid residue abolished its inhibitory potency. Moreover, when the trihydroxypropyl side chain of the sialic acid molecule was modified by periodate-borohydride treatment, the truncated C7-sialic acid was unable to bind ATN n. This result suggests that the glycerol side chain of Neu5Ac, especially the C-8 and/or C-9 portion is an important determinant for ATN n. The hemagghtination-inhibition, results using several mono-, di-, and tri-saccharides containing terminal sialic acid and various sialoglycoproteins reveals that ATN H preferentially binds the a-(2 ---, 6)-linked sialic acid. Furthermore, /3-D-GlcNAc-(1 --, 3)-[ a-NeuGc-(2 ---, 6)]-GalNAc-ol was found to be the best ligand for ATNrt.

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