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Genetic diversity of porcine reproductive and respiratory syndrome virus isolates in Flanders
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Identification of the CD163 protein domains involved in infection of the porcine reproductive and respiratory syndrome virus
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- Journal Article
- A1
- open access
The M/GP(5) glycoprotein complex of porcine reproductive and respiratory syndrome virus binds the sialoadhesin receptor in a sialic acid-dependent manner
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A variable region in GP4 of European-type porcine reproductive and respiratory syndrome virus induces neutralizing antibodies against homologous but not heterologous virus strains
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Porcine reproductive and respiratory syndrome virus entry into the porcine macrophage
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GP4-specific neutralizing antibodies might be a driving force in PRRSV evolution
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Identification of the CD163 protein domains involved in infection of the porcine reproductive and respiratory syndrome virus
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The porcine reproductive and respiratory syndrome virus requires trafficking through CD163-positive early endosomes, but not late endosomes, for productive infection
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Sialoadhesin and CD163 join forces during entry of the porcine reproductive and respiratory syndrome virus
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Porcine arterivirus attachment to the macrophage-specific receptor sialoadhesin is dependent on the sialic acid-binding activity of the N-terminal immunoglobulin domain of sialoadhesin