Relative intensities of recognition factors at two combining sites of Ralstonia solanacearum lectin (RSL) for accommodating LFuc alpha 1 ->, DMan alpha 1 -> and Gal beta 1 -> 3/4GlcNAc glycotopes

[摘要]：Owing to the weak reactivities of monomeric DMan alpha 1 -> and Gal beta 1 -> 3/4GlcNAc beta (I-beta/II beta) glycotopes with Ralstonia solanacearum lectin (RSL), their recognition roles were previously ignored. In this study, the interaction intensities of RSL toward four monomeric glycotopes LFuc alpha 1 ->, DMan alpha 1 -> and I-beta/II beta within two combining sites were established by both enzyme-linked lectinosorbent and inhibition assays. It was found that high density of LFuc alpha 1 -> complex enhanced the recognition intensities at LFuc alpha 1 -> site, polyvalent DMan alpha 1 -> was essential for binding at the DMan alpha 1 -> site and polyvalent I-beta/II beta was required at LFuc alpha 1 -> site. The peculiar recognition systems of RSL are very different from other well known microbial lectins. (C) 2012 Published by Elsevier B. V. on behalf of the Federation of European Biochemical Societies.

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