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Archives of Virology|November 4, 2009
The porcine reproductive and respiratory syndrome virus requires trafficking through CD163-positive early endosomes, but not late endosomes, for productive infectionHanne Van Gorp, Wander Van Breedam, Peter L Delputte, et al.
The Journal of General Virology|November 15, 2008
Sialoadhesin and CD163 join forces during entry of the porcine reproductive and respiratory syndrome virusHanne Van Gorp, Wander Van Breedam, Peter L Delputte, et al.
Vaccine|May 11, 2011
Characterization of antigenic regions in the porcine reproductive and respiratory syndrome virus by the use of peptide-specific serum antibodiesMerijn Vanhee, Wander Van Breedam, Sarah Costers, et al.
The Journal of General Virology|June 7, 2013
Porcine, murine and human sialoadhesin (Sn/Siglec-1/CD169): portals for porcine reproductive and respiratory syndrome virus entry into target cellsWander Van Breedam, Mieke Verbeeck, Isaura Christiaens, et al.
Veterinary Research|March 20, 2012
Demonstration of microchimerism in pregnant sows and effects of congenital PRRSV infectionUladzimir U Karniychuk, Wander Van Breedam, Nadine Van Roy, et al.
Journal of Virology|December 25, 2009
Identification of the CD163 protein domains involved in infection of the porcine reproductive and respiratory syndrome virusHanne Van Gorp, Wander Van Breedam, Jan Van Doorsselaere, et al.
The Journal of General Virology|July 26, 2017
Molecular cloning of porcine Siglec-3, Siglec-5 and Siglec-10, and identification of Siglec-10 as an alternative receptor for porcine reproductive and respiratory syndrome virus (PRRSV)Jiexiong Xie, Isaura Christiaens, Bo Yang, et al.
Virus Research|September 15, 2010
GP4-specific neutralizing antibodies might be a driving force in PRRSV evolutionSarah Costers, Merijn Vanhee, Wander Van Breedam, et al.
FEMS Microbiology Reviews|November 6, 2013
Bitter-sweet symphony: glycan-lectin interactions in virus biologyWander Van Breedam, Stefan Pöhlmann, Herman W Favoreel, et al.
Journal of Virology|June 15, 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 sialoadhesinPeter L Delputte, Wander Van Breedam, Iris Delrue, et al.
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