Role of endocytosis and cathepsin-mediated activation in Nipah virus entry.
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.
Diederich
Sandra
S
Institute of Virology, Philipps University of Marburg, Germany.
Thiel
Lena
L
Maisner
Andrea
A
D000818:Animals; D002401:Cathepsin B / Q000378:metabolism*; D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism / Q000821:virology; D004705:Endocytosis / Q000502:physiology; D036388:Ephrin-B2 / Q000378:metabolism*; D045464:Henipavirus Infections / Q000821:virology*; D006801:Humans; D045405:Nipah Virus / Q000502:physiology*; D011991:Receptors, Virus / Q000502:physiology; D014759:Viral Envelope Proteins / Q000378:metabolism; D053586:Virus Internalization
D036388:Ephrin-B2; C510755:F protein, Nipah virus; D011991:Receptors, Virus; D014759:Viral Envelope Proteins; D002401:Cathepsin B