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
| |
Author
|
|
|
|
| |
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. |
| |
Language
|
|
|
|
English
| |
Source (journal)
|
|
|
|
Journal of virology. - Baltimore, Md
| |
Publication
|
|
|
|
Baltimore, Md
:
2007
| |
ISSN
|
|
|
|
0022-538X
| |
DOI
|
|
|
|
10.1128/JVI.00569-07
| |
Volume/pages
|
|
|
|
81
:17
(2007)
, p. 9546-9550
| |
ISI
|
|
|
|
000248923700068
| |
Full text (Publisher's DOI)
|
|
|
|
| |
Full text (publisher's version - intranet only)
|
|
|
|
| |
|