Inhibition of influenza virus fusion by polyanionic proteins

Biochemical Pharmacology
P SchoenP J Swart

Abstract

Anionic charge-modified human serum albumin (HSA) has previously been shown to exert potent in vitro activity against human immunodeficiency virus type 1 (HIV-1). In these studies, introduction of the additional negative charges was performed by derivatizing the epsilon-amino groups of lysine residues with succinic (Suc-HSA) or cis-aconitic anhydride (Aco-HSA), by which primary amino groups are replaced with carboxylic acids. The anti-HIV-1 activity was related to inhibition of gp41-mediated membrane fusion. Here, we investigated the activity of aconitylated and succinylated proteins on influenza virus membrane fusion, which is mediated by the viral membrane glycoprotein hemagglutinin (HA). Aco-HSA and Suc-HSA markedly inhibited the rates and extents of fusion of fluorescently labeled virosomes bearing influenza HA, with target membranes derived from erythrocytes. The inhibitory activity was dependent on the overall negative-charge density; HSA modified with 36 or less extra negative charges failed to inhibit fusion. The inhibition of fusion showed a certain degree of specificity for the protein carrying the negative charges: polyanionic HSA and beta-lactoglobulin A derivatives had fusion-inhibitory activity, whereas succinylat...Continue Reading

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Citations

Mar 28, 2003·Biochemical and Biophysical Research Communications·Judit ReményiFerenc Hudecz
Jan 9, 2015·PLoS Pathogens·Craig N Jenne, Paul Kubes
Oct 5, 2016·Biochemical Pharmacology·T G VillaJ M Ageitos
Aug 19, 2000·Antiviral Chemistry & Chemotherapy·M Lüscher-Mattli
Mar 5, 2021·Bioconjugate Chemistry·Maria Vittoria Spanedda, Line Bourel-Bonnet

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