RELATIVE AFFINITY OF THE HUMAN PARAINFLUENZA VIRUS TYPE-3 HEMAGGLUTININ-NEURAMINIDASE FOR SIALIC-ACID CORRELATES WITH VIRUS-INDUCED FUSION ACTIVITY
RELATIVE AFFINITY OF THE HUMAN PARAINFLUENZA VIRUS TYPE-3 HEMAGGLUTININ-NEURAMINIDASE FOR SIALIC-ACID CORRELATES WITH VIRUS-INDUCED FUSION ACTIVITY
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DOI：
10.1128/jvi.67.11.6463-6468.1993
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发表时间：
1993-11-01
影响因子：
5.4
通讯作者：
PELUSO, RW
中科院分区：
文献类型：
--
作者：
MOSCONA, A;PELUSO, RW
包膜病毒引起疾病的能力取决于它们通过膜融合事件进入宿主细胞的能力。了解这些早期事件的感染，阻断感染的方法的设计至关重要，是需要在中性pH值介导膜融合的病毒，如副粘病毒和人类免疫缺陷病毒。唾液酸是人副流感病毒3型（HPF 3）血凝素-神经氨酸酶（HN）糖蛋白的受体，该分子负责病毒与细胞表面的结合。为了使融合蛋白（F）或HPF 3促进膜融合，HN必须与其受体相互作用。在本报告中，选择了两种具有增加的融合促进表型的HPF 3变体，并用于研究HN糖蛋白在膜融合中的功能。融合性的增加与HN蛋白中单个氨基酸的变化相关，该变化导致变异病毒与唾液酸受体的结合增加。这些结果表明，HN蛋白与其受体结合的亲合力调节F蛋白介导的融合水平，并开始定义副粘病毒的受体结合蛋白在膜融合过程中的一个作用。
The ability of enveloped viruses to cause disease depends on their ability to enter the host cell via membrane fusion events. An understanding of these early events in infection, crucial for the design of methods of blocking infection, is needed for viruses that mediate membrane fusion at neutral pH, such as paramyxoviruses and human immunodeficiency virus. Sialic acid is the receptor for the human parainfluenza virus type 3 (HPF3) hemagglutinin-neuraminidase (HN) glycoprotein, the molecule responsible for binding of the virus to cell surfaces. In order for the fusion protein (F) or HPF3 to promote membrane fusion, the HN must interact with its receptor. In the present report, two variants of HPF3 with increased fusion-promoting phenotypes were selected and used to study the function of the HN glycoprotein in membrane fusion. increased fusogenicity correlated with single amino acid changes in the HN protein that resulted in increased binding of the variant viruses to the sialic acid receptor. These results suggest that the avidity of binding of the HN protein to its receptor regulates the level of F protein-mediated fusion and begin to define one role of the receptor-binding protein of a paramyxovirus in the membrane fusion process.