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.
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Article Synopsis
- Lectins are proteins that have potential biological benefits, particularly in reducing inflammation and pain, which was the focus of a study evaluating their effects on zebrafish.
- The study specifically examined three plant lectins (DVL, VML, and PPL) to see if they could alleviate pain from menthol and capsaicin when injected into the fish, with the PPL lectin showing significant antinociceptive effects only against capsaicin.
- The findings suggested that not all lectins have the same pain-relieving properties, and the way they bind to carbohydrates may influence their effectiveness in reducing pain.
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