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Entry Inhibition of Influenza Viruses with High Mannose Binding Lectin ESA-2 from the Red Alga Eucheuma serra through the Recognition of Viral Hemaggl

tetano

Editor, Senior Moderator
Mar Drugs. 2015 May 29;13(6):3454-65. doi: 10.3390/md13063454.
[h=1]Entry Inhibition of Influenza Viruses with High Mannose Binding Lectin ESA-2 from the Red Alga Eucheuma serra through the Recognition of Viral Hemagglutinin.[/h] Sato Y[SUP]1[/SUP], Morimoto K[SUP]2[/SUP], Kubo T[SUP]3[/SUP], Sakaguchi T[SUP]4[/SUP], Nishizono A[SUP]5[/SUP], Hirayama M[SUP]6[/SUP], Hori K[SUP]7[/SUP].
[h=3]Author information[/h]

[h=3]Abstract[/h] Lectin sensitivity of the recent pandemic influenza A virus (H1N1-2009) was screened for 12 lectins with various carbohydrate specificity by a neutral red dye uptake assay with MDCK cells. Among them, a high mannose (HM)-binding anti-HIV lectin, ESA-2 from the red alga Eucheuma serra, showed the highest inhibition against infection with an EC50 of 12.4 nM. Moreover, ESA-2 exhibited a wide range of antiviral spectrum against various influenza strains with EC50s of pico molar to low nanomolar levels. Besides ESA-2, HM-binding plant lectin ConA, fucose-binding lectins such as fungal AOL from Aspergillus oryzae and AAL from Aleuria aurantia were active against H1N1-2009, but the potency of inhibition was of less magnitude compared with ESA-2. Direct interaction between ESA-2 and a viral envelope glycoprotein, hemagglutinin (HA), was demonstrated by ELISA assay. This interaction was effectively suppressed by glycoproteins bearing HM-glycans, indicating that ESA-2 binds to the HA of influenza virus through HM-glycans. Upon treatment with ESA-2, no viral antigens were detected in the host cells, indicating that ESA-2 inhibited the initial steps of virus entry into the cells. ESA-2 would thus be useful as a novel microbicide to prevent penetration of viruses such as HIV and influenza viruses to the host cells.


[h=4]KEYWORDS:[/h] Eucheuma serra; anti-influenza activity; high mannose glycan; lectin; red algae

PMID: 26035023 [PubMed - in process] Free full text
 
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