Abstract
The lectins DC-SIGN and DC-SIGNR can augment viral infection; however, the range of pathogens interacting with these attachment factors is incompletely defined. Here we show that DC-SIGN and DC-SIGNR enhance infection mediated by the glycoprotein (GP) of Marburg virus (MARV) and the S protein of severe acute respiratory syndrome coronavirus and might promote viral dissemination. SIGNR1, a murine DC-SIGN homologue, also enhanced infection driven by MARV and Ebola virus GP and could be targeted to assess the role of attachment factors in filovirus infection in vivo.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Cell Adhesion Molecules / physiology*
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Glycoproteins / physiology*
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Lectins, C-Type / physiology*
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Marburgvirus / physiology*
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Membrane Glycoproteins / physiology*
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Receptors, Cell Surface / physiology*
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Severe acute respiratory syndrome-related coronavirus / physiology*
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Spike Glycoprotein, Coronavirus
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Viral Envelope Proteins / physiology*
Substances
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CLEC4M protein, human
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Cell Adhesion Molecules
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DC-specific ICAM-3 grabbing nonintegrin
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Glycoproteins
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Lectins, C-Type
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Membrane Glycoproteins
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Receptors, Cell Surface
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Spike Glycoprotein, Coronavirus
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Viral Envelope Proteins
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spike glycoprotein, SARS-CoV
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spike protein, mouse hepatitis virus