Diederich Sandra, Maisner Andrea
Philipps-Universität Marburg, Institut für Virologie, Hans-Meerwein-Str 2, Marburg, Germany.
Ann N Y Acad Sci. 2007 Apr;1102:39-50. doi: 10.1196/annals.1408.003.
Nipah virus (NiV) is a highly pathogenic paramyxovirus, which emerged in 1998 from fruit bats in Malaysia and caused an outbreak of severe respiratory disease in pigs and fatal encephalitis in humans with high mortality rates. In contrast to most paramyxoviruses, NiV can infect a large variety of mammalian species. Due to this broad host range, its zoonotic potential, its high pathogenicity for humans, and the lack of effective vaccines or therapeutics, NiV was classified as a biosafety level 4 pathogen. This article provides an overview of the molecular characteristics of NiV focusing on the structure, functions, and unique biological properties of the two NiV surface glycoproteins, the receptor-binding G protein, and the fusion protein F. Since viral glycoproteins are major determinants for cell tropism and virus spread, a detailed knowledge of these proteins can help to understand the molecular basis of viral pathogenicity.
尼帕病毒（NiV）是一种高致病性副粘病毒，1998年在马来西亚从果蝠中出现，导致猪群爆发严重呼吸道疾病，并在人类中引发致命性脑炎，死亡率很高。与大多数副粘病毒不同，NiV能感染多种哺乳动物物种。由于其广泛的宿主范围、人畜共患病潜力、对人类的高致病性以及缺乏有效的疫苗或治疗方法，NiV被归类为生物安全4级病原体。本文概述了NiV的分子特征，重点介绍了两种NiV表面糖蛋白、受体结合G蛋白和融合蛋白F的结构、功能及独特生物学特性。由于病毒糖蛋白是细胞嗜性和病毒传播的主要决定因素，详细了解这些蛋白有助于理解病毒致病性的分子基础。
