Moscona A, Peluso R W
Department of Pediatrics, Mount Sinai School of Medicine, New York, NY 10029-6574, USA.
Microb Pathog. 1996 Mar;20(3):179-84. doi: 10.1006/mpat.1996.0016.
In order for the fusion protein (F) of the human parainfluenza virus type 3 (HPF3) to promote membrane fusion and viral entry, the haemagglutinin-neuraminidase (HN) glycoprotein must interact with its receptor. Sialoglycoconjugates are known to be the receptors for the HPF3 HN, however specific attachment factors or receptors for HPF3 have not been identified. In this report we describe the analysis of variants of HPF3 with increased fusion-promoting phenotypes that were selected by treatment with viral neuraminidase. The results suggest that for HPF3, the virus is specific in its use of sialic acid receptors; the majority of sialic-acid containing molecules are not targets for HPF3.
为了使人副流感病毒3型（HPF3）的融合蛋白（F）促进膜融合和病毒进入，血凝素神经氨酸酶（HN）糖蛋白必须与其受体相互作用。已知唾液酸糖缀合物是HPF3 HN的受体，然而，HPF3的特异性附着因子或受体尚未确定。在本报告中，我们描述了对经病毒神经氨酸酶处理后选择出的具有增强融合促进表型的HPF3变体的分析。结果表明，对于HPF3，该病毒在使用唾液酸受体方面具有特异性；大多数含唾液酸的分子不是HPF3的靶标。
