VML is a lectin from Vatairea macrocarpa seeds that has various biological activities. Here, we describe three
new lectin isoforms from V. macrocarpa identified through genomic DNA analysis. One of these isoforms has high similarity
to VML, while another that has noteworthy differences. We have denoted the new isoforms as VML-2, VML-3 and
VML-4. Recombinant VML (rVML) and VML-2 (rVML-2) were expressed in Escherichia coli and were anticipated to
have similar biological activity compared to native VML. Recombinant lectins were produced using a synthetic gene
strategy to improve the expression levels. We obtained two active recombinant lectin isoforms from V. macrocarpa, and
there was no significant difference between their biological activities. The conservation between carbohydrate-binding
sites of recombinant and native proteins was demonstrated by specific inhibition of hemagglutin activity by D-galactose
and lactose. However, no inhibition was observed in the presence of glucose and mannose. Our data show that the recombinant
lectins VML and VML-2 are active and capable of recognising D-galactose and lactose. Moreover, the absence of
glycosylation does not interfere with their biological activity.
Keywords: Active protein, heterologous expression, isoform, lectin, legume, recombinant.
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