Nipah virus fusion protein: influence of cleavage site mutations on the cleavability by cathepsin L, trypsin and furin.
Nipah virus (NiV), a highly pathogenic member of the Paramyxoviridae which originated from bats, encodes for a fusion (F) protein which is proteolytically processed within endosomes by cathepsin L. We show here that sequence requirements for NiV F activation differ markedly from other para- or orthomyxoviral fusion proteins. In contrast to other viral fusion proteins with monobasic cleavage sites, processing of NiV F proteins with one single basic amino acid in the cleavage peptide by exogenous trypsin is very inefficient, and introduction of a consensus sequence for furin does not result in cleavage by this ubiquitous protease. In contrast, a multibasic cleavage peptide in the NiV F protein completely impairs proteolytic processing and the generation of biological activity.
Diederich
Sandra
S
Institut für Virologie, Hans-Meerwein-Str. 2, D-35043 Marburg, Germany.
Dietzel
Erik
E
Maisner
Andrea
A
D000595:Amino Acid Sequence; D000818:Animals; D056668:Cathepsin L / Q000378:metabolism*; D002685:Chiroptera / Q000821:virology; D045683:Furin / Q000378:metabolism*; D008969:Molecular Sequence Data; D020125:Mutation, Missense; D045405:Nipah Virus / Q000235:genetics / Q000302:isolation & purification / Q000502:physiology*; D016415:Sequence Alignment; D014357:Trypsin / Q000378:metabolism*; D014759:Viral Envelope Proteins / Q000235:genetics* / Q000378:metabolism*
C510755:F protein, Nipah virus; D014759:Viral Envelope Proteins; D014357:Trypsin; D045683:Furin; D056668:Cathepsin L