Proceedings of the National Academy of Sciences · 1995 · 108 citations · 22 references
Life SciencesBiochemistryInfectious DiseasesHost-pathogen InteractionsMolecular VirologyVirologyViral AttachmentViral EntryViral InfectionsViral PathogenesisVirus EntryVirus-host InteractionsAffinity ColumnsConcentration-dependent BindingVaricella-zoster Virus InfectionsViral Entry InhibitorsViral Entry MechanismsViral Entry ReceptorsViral GlycoproteinsVirus Adsorption
Envelope glycoproteins of varicella zoster virus (VZV) contain mannose 6-phosphate (Man6P) residues. We now report that Man6P competitively and selectively inhibits infection of cells in vitro by cell-free VZV; furthermore, dephosphorylation of VZV by exposure to alkaline phosphatase rapidly destroys infectivity. Cells are also protected from VZV in a concentration-dependent manner by heparin (ED50 = 0.23 micrograms/ml; 95% confidence limits = 0.16-0.26 microgram/ml) but not by chondroitin sulfate. Both heparin and Man6P are protective only when present about the time of inoculation. Heparin but not Man6P interferes with the attachment of VZV to cell surfaces; moreover, VZV binds to heparin-affinity columns. These data are compatible with a working hypothesis, whereby VZV attaches to cell surfaces by binding to a heparin sulfate proteoglycan. This binding stabilizes VZV, making possible a low-affinity interaction with another Man6P-dependent receptor, which is necessary for viral entry.
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Integrins αvβ3 and αvβ5 promote adenovirus internalization but not virus attachment
Thomas J. Wickham, Patricia Mathias, David A. Cheresh et al. · Cell · 1993 · 2.2K citations