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J Biol Chem, Vol. 273, Issue 10, 5528-5535, March 6, 1998
From the Molecular Biophysics Unit, Indian Institute of Science,
Bangalore 560012, India
Two mannose-binding lectins, Allium
sativum agglutinin (ASA) I (25 kDa) and ASAIII (48 kDa), from
garlic bulbs have been purified by affinity chromatography followed by
gel filtration. The subunit structures of these lectins are different,
but they display similar sugar specificities. Both ASAI and ASAIII are
made up of 12.5- and 11.5-kDa subunits. In addition, a complex (136 kDa) comprising a polypeptide chain of 54 ± 4 kDa and the
subunits of ASAI and ASAIII elutes earlier than these lectins on gel
filtration. The 54-kDa subunit is proven to be alliinase, which is
known to form a complex with garlic lectins. Constituent subunits of
ASAI and ASAIII exhibit the same sequence at their amino termini. ASAI and ASAIII recognize monosaccharides in mannosyl configuration. The
potencies of the ligands for ASAs increase in the following order:
mannobiose (Man
1-3Man) < mannotriose (Man1-6Man1-3Man) 
mannopentaose 
Man9-oligosaccharide. The addition of
two GlcNAc residues at the reducing end of mannotriose or mannopentaose
enhances their potencies significantly, whereas substitution of both
1-3- and 1-6-mannosyl residues of mannotriose with GlcNAc
at the nonreducing end increases their activity only marginally.
The best manno-oligosaccharide ligand is
Man9GlcNAc2Asn, which bears several
1-2-linked mannose residues. Interaction with glycoproteins
suggests that these lectins recognize internal mannose as well as bind
to the core pentasaccharide of N-linked glycans even when
it is sialylated. The strongest inhibitors are the high
mannose-containing glycoproteins, which carry larger glycan chains.
Indeed, invertase, which contains 85% of its mannose residues in
species larger than Man20GlcNAc, exhibited the highest
binding affinity. No other mannose- or mannose/glucose-binding lectin
has been shown to display such a specificity.
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