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a Institute of Virology, Philipps University of Marburg, Germany
Key Words: Nipah virus • viral glycoproteins • G protein • fusion protein • proteolytic cleavage
Address for correspondence: Dr. Andrea Maisner, Philipps-Universität Marburg, Institut für Virologie, Hans-Meerwein-Str. 2, 35043 Marburg, Germany. Voice: 06421-28-65360; fax: 06421-28-65381. maisner{at}staff.uni-marburg.de
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.
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