S18.2 Structure-activity relationship in the interaction between influenza virus and its host cell receptor

1993 ◽  
Vol 10 (4) ◽  
pp. 327-327
Author(s):  
R. Brossmer
Keyword(s):  
Influenza Virus ◽  
Host Cell ◽  
Cell Receptor ◽  
Structure Activity Relationship ◽  
Activity Relationship ◽  
Host Cell Receptor ◽  
Structure Activity

scholarly journals Structure-activity relationship studies of lipophilic teicoplanin pseudoaglycon derivatives as new anti-influenza virus agents

2018 ◽  
Vol 157 ◽  
pp. 1017-1030 ◽  
Author(s):  
Zsolt Szűcs ◽  
Viktor Kelemen ◽  
Son Le Thai ◽  
Magdolna Csávás ◽  
Erzsébet Rőth ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Structure Activity Relationship ◽  
Activity Relationship ◽  
Structure Activity

scholarly journals Anti-influenza virus activity and structure–activity relationship of aglycoristocetin derivatives with cyclobutenedione carrying hydrophobic chains

2009 ◽  
Vol 82 (1) ◽  
pp. 89-94 ◽  
Author(s):  
Lieve Naesens ◽  
Evelien Vanderlinden ◽  
Erzsébet Rőth ◽  
József Jekő ◽  
Graciela Andrei ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Structure Activity Relationship ◽  
Activity Relationship ◽  
Structure Activity ◽  
Virus Activity ◽  
Relationship Of

scholarly journals Novel Inhibitors of Influenza Virus Fusion: Structure-Activity Relationship and Interaction with the Viral Hemagglutinin

2010 ◽  
Vol 84 (9) ◽  
pp. 4277-4288 ◽  
Author(s):  
Evelien Vanderlinden ◽  
Fusun Göktaş ◽  
Zafer Cesur ◽  
Matheus Froeyen ◽  
Mark L. Reed ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Influenza A ◽  
Mdck Cells ◽  
Structure Activity Relationship ◽  
Activity Relationship ◽  
H3n2 Virus ◽  
Wild Type Virus ◽  
Erythrocyte Hemolysis ◽  
Structure Activity ◽  
Virus Fusion

ABSTRACT A new class of N-(1-thia-4-azaspiro[4.5]decan-4-yl)carboxamide inhibitors of influenza virus hemagglutinin (HA)-mediated membrane fusion that has a narrow and defined structure-activity relationship was identified. In Madin-Darby canine kidney (MDCK) cells infected with different strains of human influenza virus A/H3N2, the lead compound, 4c, displayed a 50% effective concentration of 3 to 23 μM and an antiviral selectivity index of 10. No activity was observed for A/H1N1, A/H5N1, A/H7N2, and B viruses. The activity of 4c was reduced considerably when added 30 min or later postinfection, indicating that 4c inhibits an early step in virus replication. 4c and its congeners inhibited influenza A/H3N2 virus-induced erythrocyte hemolysis at low pH. 4c-resistant virus mutants, selected in MDCK cells, contained either a single D112N change in the HA2 subunit of the viral HA or a combination of three substitutions, i.e., R220S (in HA1) and E57K (in HA2) and an A-T substitution at position 43 or 96 of HA2. The mutants showed efficiency for receptor binding and replication similar to that of wild-type virus yet displayed an increased pH of erythrocyte hemolysis. In polykaryon assays with cells expressing single-mutant HA proteins, the E57K, A96T, and D112N mutations resulted in 4c resistance, and the HA proteins containing R220S, A96T, and D112N mutations displayed an increased fusion pH. Molecular modeling identified a binding cavity for 4c involving arginine-54 and glutamic acid-57 in the HA2 subunit. Our studies with the new fusion inhibitor 4c confirm the importance of this HA region in the development of influenza virus fusion inhibitors.

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