Virology. 1992 Oct;190(2):569-78. Unique Identifier : AIDSLINE
The envelope glycoprotein of feline immunodeficiency virus (FIV)
consists of two noncovalently associated subunits, the surface
glycoprotein (SU; gp95) and the transmembrane glycoprotein (TM; gp40).
An unusual feature of the open reading frame (ORF) encoding the FIV
glycoprotein is the presence of an unusually long amino terminal
sequence (149 amino acids, L region or n-region of the signal sequence)
preceding the predicted hydrophobic signal sequence. To examine the role
of this n-region in the biosynthesis of gp95, the gene-encoding signal
sequence and the surface glycoprotein (gp95) were expressed using
recombinant vaccinia viruses. Glycoprotein mutants were constructed with
25, 42, 73, 102, and 147 amino acids removed from the n-region.
Expression studies revealed that deletion of 25-102 amino acids did not
appreciably effect the biosynthesis, intracellular transport, and
release of gp95 from the cell surface. In contrast, removal of 147 of
149 amino acids resulted in the gp95 that was blocked in release from
the cell. These results indicate that between 3 and 47 amino acids of
the n-region are required for the proper biosynthesis, processing, and
release of the FIV gp95 from infected cells.
Base Sequence Cloning, Molecular Gene Products,
env/BIOSYNTHESIS/*GENETICS/METABOLISM Hela Cells Human
Immunodeficiency Virus, Feline/*GENETICS Molecular Sequence Data
Mutagenesis/GENETICS Polymerase Chain Reaction Recombinant Fusion
Proteins/BIOSYNTHESIS/*GENETICS/METABOLISM Signal
Peptides/BIOSYNTHESIS/*GENETICS/METABOLISM Support, Non-U.S. Gov't
Support, U.S. Gov't, P.H.S. Vaccinia Virus/GENETICS JOURNAL ARTICLE