El-Deeb Ibrahim M, Guillon Patrice, Dirr Larissa, von Itzstein Mark
Institute for Glycomics , Griffith University , Gold Coast Campus , Queensland 4222 , Australia . Email:
Medchemcomm. 2016 Oct 5;8(1):130-134. doi: 10.1039/c6md00519e. eCollection 2017 Jan 1.
Human parainfluenza virus type-3 is a leading cause of acute respiratory infection in infants and children. There is currently neither vaccine nor clinically effective treatment for parainfluenza virus infection. Hemagglutinin-neuraminidase glycoprotein is a key protein in viral infection, and its inhibition has been a target for inhibitor development. In this study, we explore the structural features required for Neu2en derivatives to efficiently lock-open the 216-loop of the human parainfluenza virus type-3 hemagglutinin-neuraminidase protein.
人副流感病毒3型是婴幼儿急性呼吸道感染的主要病因。目前针对副流感病毒感染既没有疫苗也没有临床有效的治疗方法。血凝素-神经氨酸酶糖蛋白是病毒感染中的关键蛋白，对其进行抑制一直是抑制剂研发的目标。在本研究中，我们探究了Neu2en衍生物有效锁定开放人副流感病毒3型血凝素-神经氨酸酶蛋白216环所需的结构特征。
