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
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
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DOI：
10.1128/jvi.00569-07
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发表时间：
2007-09-01
影响因子：
5.4
通讯作者：
Nauwynck, Hans J.
中科院分区：
文献类型：
--
作者：
Delputte, Peter L.;Van Breedam, Wander;Nauwynck, Hans J.
唾液酸结合凝集素（sialoadhesin，Sn）是猪繁殖与呼吸综合征病毒（porcine reproductive and respiratory syndrome virus，PRRSV）的巨噬细胞限制性受体。为了研究pSn唾液酸结合活性对PRRSV感染的重要性，在预测的pSn唾液酸结合结构域中引入R-116-至-E突变，产生不能结合唾液酸的突变体pSn（RE）。PSn而不是pSn（RE）允许PRRSV结合和内化。这些数据表明pSn的唾液酸结合活性对于PRRSV附着到pSn是必需的，因此将Sn的可变N-末端结构域鉴定为PRRSV结合结构域。
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.