Abstract
PSL1a is a lectin from the mushroom Polyporus squamosus that binds to sialylated glycans and glycoconjugates with high specificity and selectivity. In addition to its N-terminal carbohydrate-binding domain, PSL1a possesses a Ca2+-dependent proteolytic activity in the C-terminal domain. In the present study, we demonstrate that PSL1a has cytotoxic effects on mammalian cancer cells, and we show that the cytotoxicity is dependent on the cysteine protease activity. PSL1a treatment leads to cell rounding and detachment from the substratum, concomitant with disruption of vinculin complexes in focal adhesions. We also demonstrate that PSL1a inhibits protein synthesis and induces apoptosis in HeLa cells, in a time- and concentration-dependent manner.
Highlights
Lectins are carbohydrate-binding proteins or glycoproteins that contain at least one carbohydrate-binding domain [1]
We further demonstrate that PSL1a leads to inhibition of protein synthesis and induction of apoptosis, but not autophagy
The primary goal of our study was to investigate the cytotoxic potential of PSL1a and to examine the possible correlation between the proteolytic activity of PSL1a and its cytotoxicity in mammalian cells
Summary
Lectins are carbohydrate-binding proteins or glycoproteins that contain at least one carbohydrate-binding domain [1]. The carbohydrate-binding domain plays an important role in recognition and reversible binding to diverse glycotopes [2]. Lectins are widely distributed in nature and have been isolated from archaea to bacteria [5, 6], viruses [7], animals [8], plants and yeasts [9, 10]. These proteins play an important role in various biological processes, such as cell signaling, protein trafficking, and carcinogenesis [11, 12]
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