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Title: Role of endocytosis and cathepsin-mediated activation in Nipah virus entry

Journal Article · · Virology
;  [1];  [1]
  1. Institute of Virology, Philipps University of Marburg (Germany)

The recent discovery that the Nipah virus (NiV) fusion protein (F) is activated by endosomal cathepsin L raised the question if NiV utilize pH- and protease-dependent mechanisms of entry. We show here that the NiV receptor ephrin B2, virus-like particles and infectious NiV are internalized from the cell surface. However, endocytosis, acidic pH and cathepsin-mediated cleavage are not necessary for the initiation of infection of new host cells. Our data clearly demonstrate that proteolytic activation of the NiV F protein is required before incorporation into budding virions but not after virus entry.

OSTI ID:
21140996
Journal Information:
Virology, Vol. 375, Issue 2; Other Information: DOI: 10.1016/j.virol.2008.02.019; PII: S0042-6822(08)00106-2; Copyright (c) 2008 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0042-6822
Country of Publication:
United States
Language:
English