As part of the human host immune responses, the glycans of the coronavirus spike protein subunits are recognized by dendritic cells [11] in the blood which binds to the glycan and subsequently expresses CD4+ and CD8+ glycopeptides. These glycopeptides label the spike protein and this labeled protein is then presented to T-cells [12]. T-cells subsequently recognize the labels, phagocytose these antigen-marked viruses, and degrade them. It has been found that the glycan-binding proteins, also known as lectins [5], can impart broad-spectrum binding properties against HIV-1, SARS-CoV, and human cytomegalovirus. The lectin which is capable of showing broad interaction via oligomannosyl antigens is known as lectin GNA (Galanthus nivalis agglutinin). The N-oligomannosyl cores are embedded in N-glycans which are commonly expressed on the surface of numerous viral pathogens [13]. Once the lectin binds to the glycan, the virus structure may undergo conformational changes that result in the fusion of the virus and host to facilitate virus entry. S-proteins are specifically responsible for host cell entry by coronaviruses [14]. Figure 1 depicts a simplified entry mechanism of the viruses into host cells.