Suppression of influenza virus infection by an N-thioacetylneuraminic acid acrylamide copolymer resistant to neuraminidase

We have previously shown that α-2-O-methyl-5-N-thioacetylneuraminic acid (α-Neu5thioAc2Me) has a higher affinity to bromelain-treated hemagglutinin (HA) of influenza A virus than sialic acid from natural sources (Machytka et al., 1993, FEBS Lett. 334, 117-120). We have now compared the inhibitory ef...

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Hauptverfasser: Itoh, Masae (VerfasserIn) , Hetterich, Peter (VerfasserIn) , Isecke, Rainer (VerfasserIn) , Brossmer, Reinhard (VerfasserIn) , Klenk, Hans-Dieter (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 1 October 1995
In: Virology
Year: 1995, Jahrgang: 212, Heft: 2, Pages: 340-347
ISSN:1096-0341
DOI:10.1006/viro.1995.1491
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1006/viro.1995.1491
Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S0042682285714912
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Verfasserangaben:Masae Itoh, Peter Hetterich, Rainer Isecke, Reinhard Brossmer, Hans-Dieter Klenk

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520 |a We have previously shown that α-2-O-methyl-5-N-thioacetylneuraminic acid (α-Neu5thioAc2Me) has a higher affinity to bromelain-treated hemagglutinin (HA) of influenza A virus than sialic acid from natural sources (Machytka et al., 1993, FEBS Lett. 334, 117-120). We have now compared the inhibitory effects of α-Neu5thioAc2Me and other sialic acid analogs on receptor binding and plaque formation of intact influenza A viruses. When α-Neu5thioAc2Me was polymerized by conjugation to polyacrylamide, its affinity to HA increased 103-fold. When analyzed by plaque reduction, the α-Neu5thioAc2 polymer was about 10 times more efficient as an inhibitor of virus replication than the α-Neu5Ac2 polymer, stressing the importance of sulfur at C5. The S-glycoside α-2-S-methyl-5-N-thioacetylneuraminic acid (α-Neu5thioAc2SMe) had the same affinity to HA as α-Neu5thioAc2Me, but was resistant to neuraminidase. The α-Neu5thioAc2S polymer interfered with the replication of a wider spectrum of influenza A virus subtypes than the α-Neu5thioAc2 polymer. The results indicate that the αNeu5thioAc2S polymer has the potential to be used as an inhibitor of influenza virus infection. 
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