The Antiviral Potential of Algal Lectins

Abstract

Algae have emerged as fascinating subjects of study due to their vast potential as sources of valuable metabolites with diverse biotechnological applications, including their use as fertilizers, feed, food, and even pharmaceutical precursors. Among the numerous compounds found in algae, lectins have garnered special attention for their unique structures and carbohydrate specificities, distinguishing them from lectins derived from other sources. Here, a comprehensive overview of the latest scientific and technological advancements in the realm of algal lectins with a particular focus on their antiviral properties is provided. These lectins have displayed remarkable effectiveness against a wide range of viruses, thereby holding great promise for various antiviral applications. It is worth noting that several alga species have already been successfully commercialized for their antiviral potential. However, the discovery of a diverse array of lectins with potent antiviral capabilities suggests that the field holds immense untapped potential for further expansion. In conclusion, algae stand as a valuable and versatile resource, and their lectins offer an exciting avenue for developing novel antiviral agents, which may lead to the development of cutting-edge antiviral therapies.

Keywords: bioactive compounds; lectins; macroalgae; marine biotechnology; mechanisms of action; microalga; seaweed; virus.

Figure 1

The structure of Griffithsin and the domains of this protein. Amino acids located within beta strands are highlighted in magenta to indicate their secondary structure, while each monomer of the domain-swapped dimer is depicted in blue. The crystal structure of a GRFT dimer with six mannoses is depicted, with each GRFT monomer shown in blue, and the N-terminal extension resulting from the cloning procedure colored in orange. Adapted from Pubmed and Micewicz et al. [41] (PDB entry code 2GTY).

Figure 2

The structure of Cyanovirin and its domains. The protein, consisting of 101 amino acids, is depicted in blue, with its β-strands and helical turns also highlighted in blue. The stereo view shows superpositions of the ensemble of the final 40 simulated annealing structures of cyanovirin-N. The backbone is shown in magenta, the disulfide bridges are depicted in orange, and all other side chains are represented in blue. Adapted from Pubmed and Botos et al. [50] (PDB entry code 1M5J).

Figure 3

The structure and domains of scytovirin. Structural domain 1 is represented in blue, structural domain 2 is represented in purple, and the disulfide bonds are highlighted in magenta. Adapted from Pubmed and Moulaei et al. [59] (PDB entry code 2JMVJ).

Figure 4

Structure and domains of microvirin. The structure is divided into two structural domains, depicted in blue and magenta, while the bound glycan is colored in orange. The insertion of four amino acids in domain A, as compared to domain B, is indicated in blue and magenta. Adapted from Pubmed and Shahzad-ul-Hussan et al. [61] (PDB entry code 2y1s).