Abstract
The present study evaluates the antiviral activity of banana lectin (BanLec) against herpes simplex virus type 1 and 2 (HSV-1 and HSV-2). Lectin was isolated from the ripen pulp of bananas (Musa paradisiaca). The study showed that lectin exhibited hemagglutination activity towards human erythrocytes A, B, AB and O group. The molecular weight of BanLec using SDS gel-electrophoresis was found to be 14,000-30,000 Da. Cytotoxicity of BanLec on the Vero cell lines showed an inhibitory concentration of 172.7 µg/mL. BanLec was virucidal and showed no cytotoxicity at the concentration tested. The lectin showed a dose-dependent antiviral activities, inhibiting HSV-1 by 16.0 µg/mL with selectivity index 10.8 and HSV-2 inhibition by 67.7 µg/mL with selectivity index 2.6. These results corroborate that BanLec could be a rich source of potential antiviral compound for HSV-1 when compared to HSV-2.
Highlights
Lectins are a unique and heterologous class of proteins with the ability to recognize and reversibly bind a variety of sugar structures present on the cell surface (Santos et al, 2014)
The fraction that gave the highest agglutination activity, peak (3) lectin was taken for the entire study
From the data obtained from MTT assay for antiviral action of banana lectin (BanLec) against the Herpes simplex virus (HSV)-1 strain, the dose that inhibited viral infection by 50% (EC50), the effective concentration required to inhibit 50% virus infection with 12.5, 25, 50, and 100 μg/mL of lectin was determined by plotting the graph against the inhibition of the virus yield versus the concentration of lectin by GravPad Prism (Figure 4)
Summary
Lectins are a unique and heterologous class of proteins with the ability to recognize and reversibly bind a variety of sugar structures present on the cell surface (Santos et al, 2014) They are found in a wide range of organisms, from viruses and bacteria to animals, plants, and humans (Mitchell et al, 2017). They have important biological functions in the organisms, including cell-cell interaction, protection from pathogens, cell adhesion, and intracellular translocation of glycoproteins, and they act as storage proteins (Yamashita et al, 1999; Jiang et al, 2006; Wang et al, 2007). You must attribute the work in the manner specified by the author or licensor
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