Abstract
The sialic acid-binding lectin sialoadhesin (Sn) is a macrophage-restricted receptor for porcine reproductive and respiratory syndrome virus (PRRSV). To investigate the importance of pSn sialic acid-binding activity for PRRSV infection, an R(116)-to-E mutation was introduced in the predicted sialic acid-binding domain of pSn, resulting in a mutant, pSn(RE), that could not bind sialic acids. PSn, but not pSn(RE), allowed PRRSV binding and internalization. These data show that the sialic acid-binding activity of pSn is essential for PRRSV attachment to pSn and thus identifies the variable, N-terminal domain of Sn as a PRRSV binding domain.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Substitution / genetics
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Animals
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Binding Sites / genetics
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CHO Cells
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Cricetinae
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Cricetulus
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Macrophages / virology*
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Membrane Glycoproteins / chemistry
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Membrane Glycoproteins / genetics
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Membrane Glycoproteins / metabolism*
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Mutagenesis, Site-Directed
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Mutation, Missense
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N-Acetylneuraminic Acid / metabolism*
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Porcine respiratory and reproductive syndrome virus / physiology*
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Protein Binding
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Protein Structure, Tertiary
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Receptors, Immunologic / chemistry
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Receptors, Immunologic / genetics
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Receptors, Immunologic / metabolism*
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Receptors, Virus / genetics
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Receptors, Virus / metabolism*
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Sialic Acid Binding Ig-like Lectin 1
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Virus Attachment*
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Virus Internalization
Substances
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Membrane Glycoproteins
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Receptors, Immunologic
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Receptors, Virus
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Sialic Acid Binding Ig-like Lectin 1
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N-Acetylneuraminic Acid