Lentil lectin has potent anti-SARS-CoV-2 activity against mutant strains and epidemic variants. 

A group from National Institutes for Food and Drug Control (NIFDC), Beijing, China, etc. has reported that lentil lectin has potent anti-SARS-CoV-2 activity against mutant strains and epidemic variants.
https://www.tandfonline.com/doi/full/10.1080/22221751.2021.1957720

A pseudovirus based neutralization assay was performed on Huh7 cells by preincubating SARS-CoV-2 pseudoviruse with lectins. WGA, lentil lectin, PHA-L and PHA-E showed most potent antiviral activity against SARS-CoV-2 pseudovirus with IC50 range from 8.5 μg/mL to 22.0 μg/mL.

Hemagglutination and cytotoxicity activity of lectins are always problematic in practical applications. PHA-L and PHA-E showed hemagglutination activity at 3.91 μg/mL, and WGA showed it at 7.81 μg/mL. The lentil lectin showed weak hemagglutination activity at the highest concentrations tested (at 1 mg/mL). Cytotoxicity was evaluated with using Huh7 or 293T cells in 96-well plates and incubated at 37°C for 24 h. These lectins showed no cytotoxicity at 500 μg/mL.

Taking these things into consideration, lentil lectin would be more suitable to be a candidate as SARS-CoV-2 inhibitor.

It is of note that elimination of individual N- or O-linked glycosylation site on SARS-CoV-2 S protein had no influence on neutralization susceptibility to lentil lectin, suggesting that lentil lectin may bind to glycans at multiple sites on S trimer. The lentil lectin has strong binding to both oligomannose-type glycans (Man-5 to Man-9), and N-glycans containing GlcNAc at the non-reducing end terminus including both the complex- and hybrid-type glycans.

Glycosylation sites at N165, N234 and N343 were located around the RBD, and the majority of glycans at these three sites are lentil lectin binding glycans, especially the glycans at N234 are totally oligomannose-type which could be efficiently bound by lentil lectin. Interestingly, removal of any one of glycosylation sites at N165, N234 and N343 had no effect on neutralization susceptibility to lentil lectin, suggesting that the existence of two of these glycosylation sites could support neutralization by lentil lectin.

Although a number of mutations have been emerging, glycosylation sites at N165, N234 and N343 were 100% conserved so far. Therefore, the use of lentil lectin might to be a GOOD selectin because of its high tolerance for SARS-CoV-2 variants.