Abstract
A lectin-like protein of unknown function designated as LSMT was recently discovered in the edible mushroom Agaricus bisporus. The protein shares high structural similarity to HA-33 from Clostridium botulinum (HA33) and Ricin-B-like lectin from the mushroom Clitocybe nebularis (CNL), which have been developed as drug carrier and anti-cancer, respectively. These homologous proteins display the ability to penetrate the intestinal epithelial cell monolayer, and are beneficial for oral administration. As the characteristics of LSMT are unknown, a structural study in silico was performed to assess its potential pharmaceutical application. The study suggested potential binding to target ligands such as HA-33 and CNL although the nature, specificity, capacity, mode, and strength may differ. Further molecular docking experiments suggest that interactions between the LSMT and tested ligands may take place. This finding indicates the possible use of the LSMT protein, initiating new research on its use for pharmaceutical purposes.
Highlights
Proteins of Lectin family have been assessed for application as drug carrier because of their capability to recognize and bind sugar moieties
Lectin from mushroom A. bisporus has been developed as an anti-cancer agent [23], for demonstrating inhibition to proliferation of epithelial cell of the colon. During evaluation of their amino acid sequences, the carbohydrate-binding residues in HA-33 from Clostridium botulinum (HA33) and Clitocybe nebularis (CNL) appeared to be not conserved in light subunit of mushroom tyrosinase (LSMT) [27, 33], binding to carbohydrate or attachment to cell wall was proposed to be unlikely [17]
Our effort to isolate LSMT is fruitless whilst preparing its recombinant version would be hampered by validation of the gene product
Summary
Proteins of Lectin family have been assessed for application as drug carrier because of their capability to recognize and bind sugar moieties. During evaluation of their amino acid sequences, the carbohydrate-binding residues in HA33 and CNL appeared to be not conserved in LSMT [27, 33], binding to carbohydrate or attachment to cell wall was proposed to be unlikely [17]. The secondary structures of CNL, HA-33, and LSMT in that region are similar thereby potential interactions could be predicted (Figure 1a–d). Predicted potential ligand molecules in the binding site region LSMT, ligand binding-sites of CNL and HA-33 are indicated by an NAG molecule (in stick) in the superimposed structures (D).
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