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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

(2007) JOURNAL OF VIROLOGY. 81(17). p.9546-9550
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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.
Keywords
INFECTION, RESPIRATORY SYNDROME VIRUS, DIFFERENTIATION, IDENTIFICATION, LELYSTAD VIRUS, PRRSV, ALVEOLAR MACROPHAGES, MONOCLONAL-ANTIBODIES, SITE-DIRECTED MUTAGENESIS, MYSTERY SWINE DISEASE

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Citation

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Chicago
Delputte, Peter, Wander Van Breedam, Iris Delrue, Cornelia Oetke, Paul R Crocker, and Hans Nauwynck. 2007. “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.” Journal of Virology 81 (17): 9546–9550.
APA
Delputte, P., Van Breedam, W., Delrue, I., Oetke, C., Crocker, P. R., & Nauwynck, H. (2007). 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. JOURNAL OF VIROLOGY, 81(17), 9546–9550.
Vancouver
1.
Delputte P, Van Breedam W, Delrue I, Oetke C, Crocker PR, Nauwynck H. 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. JOURNAL OF VIROLOGY. 2007;81(17):9546–50.
MLA
Delputte, Peter, Wander Van Breedam, Iris Delrue, et al. “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.” JOURNAL OF VIROLOGY 81.17 (2007): 9546–9550. Print.
@article{378947,
  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.},
  author       = {Delputte, Peter and Van Breedam, Wander and Delrue, Iris and Oetke, Cornelia and Crocker, Paul R and Nauwynck, Hans},
  issn         = {0022-538X},
  journal      = {JOURNAL OF VIROLOGY},
  language     = {eng},
  number       = {17},
  pages        = {9546--9550},
  title        = {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},
  url          = {http://dx.doi.org/10.1128/JVI.00569-07},
  volume       = {81},
  year         = {2007},
}

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