scholarly journals An IgM antibody targeting the receptor binding site of influenza B blocks viral infection with great breadth and potency

Theranostics ◽  
2019 ◽  
Vol 9 (1) ◽  
pp. 210-231 ◽  
Author(s):  
Chenguang Shen ◽  
Minwei Zhang ◽  
Yuanzhi Chen ◽  
Limin Zhang ◽  
Guosong Wang ◽  
...  
Keyword(s):  
Viral Infection ◽  
Binding Site ◽  
Receptor Binding ◽  
Influenza B ◽  
Receptor Binding Site ◽  
Igm Antibody ◽  
Great Breadth ◽  
Antibody Targeting

A multimechanistic antibody targeting the receptor binding site potently cross-protects against influenza B viruses

2017 ◽  
Vol 9 (412) ◽  
pp. eaam5752 ◽  
Author(s):  
Chenguang Shen ◽  
Junyu Chen ◽  
Rui Li ◽  
Mengya Zhang ◽  
Guosong Wang ◽  
...  
Keyword(s):  
Binding Site ◽  
Receptor Binding ◽  
Influenza B ◽  
Receptor Binding Site ◽  
Antibody Targeting

scholarly journals Potent sialic acid inhibitors that target influenza A virus hemagglutinin

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Yu-Jen Chang ◽  
Cheng-Yun Yeh ◽  
Ju-Chien Cheng ◽  
Yu-Qi Huang ◽  
Kai-Cheng Hsu ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Antiviral Activity ◽  
Binding Site ◽  
Influenza A Virus ◽  
Receptor Binding ◽  
Influenza A ◽  
The United States ◽  
Ligand Complex ◽  
Receptor Binding Site ◽  
Computational Strategy

AbstractEradicating influenza A virus (IAV) is difficult, due to its genetic drift and reassortment ability. As the infectious cycle is initiated by the influenza glycoprotein, hemagglutinin (HA), which mediates the binding of virions to terminal sialic acids moieties, HA is a tempting target of anti-influenza inhibitors. However, the complexity of the HA structure has prevented delineation of the structural characterization of the HA protein–ligand complex. Our computational strategy efficiently analyzed > 200,000 records of compounds held in the United States National Cancer Institute (NCI) database and identified potential HA inhibitors, by modeling the sialic acid (SA) receptor binding site (RBS) for the HA structure. Our modeling revealed that compound NSC85561 showed significant antiviral activity against the IAV H1N1 strain with EC50 values ranging from 2.31 to 2.53 µM and negligible cytotoxicity (CC50 > 700 µM). Using the NSC85561 compound as the template to generate 12 derivatives, robust bioassay results revealed the strongest antiviral efficacies with NSC47715 and NSC7223. Virtual screening clearly identified three SA receptor binding site inhibitors that were successfully validated in experimental data. Thus, our computational strategy has identified SA receptor binding site inhibitors against HA that show IAV-associated antiviral activity.

Nicotinic receptor binding site probed with unnatural amino acid incorporation in intact cells

Science ◽  
1995 ◽  
Vol 268 (5209) ◽  
pp. 439-442 ◽  
Author(s):  
M. Nowak ◽  
P. Kearney ◽  
Sampson ◽  
M. Saks ◽  
C. Labarca ◽  
...  
Keyword(s):  
Amino Acid ◽  
Binding Site ◽  
Receptor Binding ◽  
Nicotinic Receptor ◽  
Unnatural Amino Acid ◽  
Amino Acid Incorporation ◽  
Receptor Binding Site ◽  
Intact Cells ◽  
Acid Incorporation
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