PMID- 17567703
OWN - NLM
STAT- MEDLINE
DCOM- 20070928
LR  - 20181113
IS  - 0022-538X (Print)
IS  - 1098-5514 (Electronic)
IS  - 0022-538X (Linking)
VI  - 81
IP  - 17
DP  - 2007 Sep
TI  - 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.
PG  - 9546-50
AB  - 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.
FAU - Delputte, Peter L
AU  - Delputte PL
AD  - Laboratory of Virology, Department Virology, Parasitology, and Immunology, Ghent 
      University, Salisburylaan 133, B-9820 Merelbeke, Belgium. peter.delputte@UGent.be
FAU - Van Breedam, Wander
AU  - Van Breedam W
FAU - Delrue, Iris
AU  - Delrue I
FAU - Oetke, Cornelia
AU  - Oetke C
FAU - Crocker, Paul R
AU  - Crocker PR
FAU - Nauwynck, Hans J
AU  - Nauwynck HJ
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20070613
PL  - United States
TA  - J Virol
JT  - Journal of virology
JID - 0113724
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Receptors, Immunologic)
RN  - 0 (Receptors, Virus)
RN  - 0 (Sialic Acid Binding Ig-like Lectin 1)
RN  - GZP2782OP0 (N-Acetylneuraminic Acid)
SB  - IM
MH  - Amino Acid Substitution/genetics
MH  - Animals
MH  - Binding Sites/genetics
MH  - CHO Cells
MH  - Cricetinae
MH  - Cricetulus
MH  - Macrophages/*virology
MH  - Membrane Glycoproteins/chemistry/genetics/*metabolism
MH  - Mutagenesis, Site-Directed
MH  - Mutation, Missense
MH  - N-Acetylneuraminic Acid/*metabolism
MH  - Porcine respiratory and reproductive syndrome virus/*physiology
MH  - Protein Binding
MH  - Protein Structure, Tertiary
MH  - Receptors, Immunologic/chemistry/genetics/*metabolism
MH  - Receptors, Virus/genetics/*metabolism
MH  - Sialic Acid Binding Ig-like Lectin 1
MH  - *Virus Attachment
MH  - Virus Internalization
PMC - PMC1951444
EDAT- 2007/06/15 09:00
MHDA- 2007/09/29 09:00
PMCR- 2008/01/01
CRDT- 2007/06/15 09:00
PHST- 2007/06/15 09:00 [pubmed]
PHST- 2007/09/29 09:00 [medline]
PHST- 2007/06/15 09:00 [entrez]
PHST- 2008/01/01 00:00 [pmc-release]
AID - JVI.00569-07 [pii]
AID - 0569-07 [pii]
AID - 10.1128/JVI.00569-07 [doi]
PST - ppublish
SO  - J Virol. 2007 Sep;81(17):9546-50. doi: 10.1128/JVI.00569-07. Epub 2007 Jun 13.