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Inhibition of herpes simplex virus infection by lactoferrin is dependent on interference with the virus binding to glycosaminoglycans.

Journal article
Authors Magda Marchetti
Edward Trybala
Fabiana Superti
Maria Johansson
Tomas Bergström
Published in Virology
Volume 318
Issue 1
Pages 405-13
ISSN 0042-6822
Publication year 2004
Published at Institute of Laboratory Medicine, Dept of Clinical Virology
Pages 405-13
Language en
Links dx.doi.org/10.1016/j.virol.2003.09....
Keywords Animals, Antiviral Agents, metabolism, pharmacology, Cattle, Cells, Cultured, Chondroitin Sulfates, metabolism, Fibroblasts, drug effects, virology, Glycosaminoglycans, chemistry, metabolism, Heparitin Sulfate, metabolism, Herpesvirus 1, Human, drug effects, metabolism, pathogenicity, Humans, L Cells (Cell Line), Lactoferrin, metabolism, pharmacology, Mice, Viral Envelope Proteins, metabolism
Subject categories Medical and Health Sciences

Abstract

Previous reports have indicated that lactoferrin inhibits herpes simplex virus (HSV) infection during the very early phases of the viral replicative cycle. In the present work we investigated the mechanism of the antiviral activity of lactoferrin in mutant glycosaminoglycan (GAG)-deficient cells. Bovine lactoferrin (BLf) was a strong inhibitor of HSV-1 infection in cells expressing either heparan sulfate (HS) or chondroitin sulfate (CS) or both, but was ineffective or less efficient in GAG-deficient cells or in cells treated with GAG-degrading enzymes. In contrast to wild-type HSV-1, virus mutants devoid of glycoprotein C (gC) were significantly less inhibited by lactoferrin in GAG-expressing cells, indicating that lactoferrin interfered with the binding of viral gC to cell surface HS and/or CS. Finally, we demonstrated that lactoferrin bound directly to both HS and CS isolated from surfaces of the studied cells, as well as to commercial preparations of GAG chains. The results support the hypothesis that the inhibition of HSV-1 infectivity by lactoferrin is dependent on its interaction with cell surface GAG chains of HS and CS.

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