Involvement of a highly polyvalent Glycan in the cell-binding of the aggregation factor from the marine spongeMicrociona prolifera

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Abstract
A proteoglycan-like aggregation factor from the marine spongeMicrociona prolifera (MAF) mediates cell-cell recognition via a cell-binding and a self-association domain. After repetitive and prolonged treatment of MAF with glycopeptide-N-glycosidase (PNGase) the specific binding of MAF to homotypic cells was decreased by 72%. Polyacrylamide gel electrophoresis and gel filtration analysis of such PNGase digests showed that: (1) the enzyme released a single glycan type of Mr = 6 × 1032 (G-6) from MAF, (2) 1 mole of MAF contains at least 830 moles of N-linked chains of G-6 glycan. The correlation between the loss of the binding activity of MAF and the extent of the release of the repetitive G-6 polysaccharide strongly suggests its involvement in MAF-cell association via highly polyvalent interactions.